Infrared spectroscopy of proteins

Barth, Andreas

doi:10.1016/j.bbabio.2007.06.004

Cited by 5,129Spectroscopy Techniques in Biomedical and Chemical ResearchProtein Structure and DynamicsSpectroscopy and Quantum Chemical Studies

Infrared spectroscopy of proteins

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Barth, Andreas·2007·Biochimica et Biophysica Acta (BBA) - Bioenergetics

DOI 10.1016/j.bbabio.2007.06.004

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Abstract

This review discusses the application of infrared spectroscopy to the study of proteins. The focus is on the mid-infrared spectral region and the study of protein reactions by reaction-induced infrared difference spectroscopy.

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The Amide I normal mode of vibration is mainly peptide-backbone C=O stretching (~80%) and N-H bending (~20%) and is highly sensitive to protein structural changes.
“The Amide I normal mode of vibration is mainly to peptide-backbone C=O stretching (∼80 % of the mode) and N–H bending (∼20 % of the mode) adsorptions and it is highly sensitive to protein structural changes [57].”
From Ferritin adsorption onto chrysotile asbestos fibers influences the protein secondary structure (2024) · cites this paper as [57]

Introduction to Infrared and Raman Spectroscopy
(1975) · Elsevier eBooks · doi:10.1016/b978-0-12-182552-2.x5001-3 · Cited by 5,474 · cited 7× · see citing works
“Only the strongest bands are listed in Table 1, or 724 – 1174 Couples with adjacent CH 2 groups, in phase mode at 724 cm − 1 most intense [79] Extended and corrected version of a previous compilation [150].”
BackgroundInfluential
Relationships between the carbon-oxygen stretching frequencies of carboxylato complexes and the type of carboxylate coordination
Deacon, G. B. (1980) · Coordination Chemistry Reviews · doi:10.1016/s0010-8545(00)80455-5 · Cited by 5,139 · cited 1× · see citing works
“Examples are (i) the two coupled CO vibrations in the COO − group which make the carboxylate absorption sensitive to the mode of cation chelation [95 – 97] and has been used in studies of several Ca 2+ binding proteins [98,99]; (ii) the sensitivity of P \ O or V \ O stretching vibrations of…”
Method
Examination of the secondary structure of proteins by deconvolved FTIR spectra
Byler, D. M., & Susi, H. (1986) · Biopolymers · doi:10.1002/bip.360250307 · Cited by 3,003 · cited 1× · see citing works
“The two most common approaches to determine the secondary structure are: (i) fitting the amide I band with component bands [10,220,228] after identifying their position with band narrowing techniques [229 – 232] and (ii) decomposing the amide I band into basis spectra which have been calculated…”
Method
Handbook of Vibrational Spectroscopy
(2006) · Wiley eBooks · doi:10.1002/0470027320 · Cited by 2,985 · see citing works
Vibrational Spectroscopy and Conformation of Peptides, Polypeptides, and Proteins
Krimm, S., & Bandekar, J. (1986) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60528-8 · Cited by 2,856 · cited 9× · see citing works
“The amide II band is weak or absent in the Raman spectrum [151].”
BackgroundInfluential
What vibrations tell about proteins
Barth, A., & Zscherp, C. (2002) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583502003815 · Cited by 2,088 · see citing works
Self-citation
The Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
Jackson, M., & Mantsch, H. H. (1995) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409239509085140 · Cited by 2,040 · cited 1× · see citing works
“Probably the most common application of infrared spectroscopy in protein studies is the analysis of secondary structure [1,3,4,6,8 – 10, 221, 222 ].”
Background
Anoxygenic Photosynthetic Bacteria
Blankenship, R. E., Bauer, C. E., & Madigan, M. T. (1995) · Advances in photosynthesis and respiration · doi:10.1007/0-306-47954-0 · Cited by 1,912 · see citing works
Handbook of vibrational spectroscopy
Chalmers, J. M., & Griffiths, P. R. (2002) · Cited by 1,823 · see citing works
Internal Reflection Spectroscopy
Harrick, N. J., & Hoffman, J. G. (1968) · Physics Today · doi:10.1063/1.3034675 · Cited by 1,725 · see citing works
Hydrogen exchange and structural dynamics of proteins and nucleic acids
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“Thus every encounter of an acidic side chain group with OH − will abstract the side chain proton while on average 1000 collisions are needed to deprotonate an amide group [250].”
BackgroundInfluential
The infrared absorption of amino acid side chains
Barth, A. (2000) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(00)00021-3 · Cited by 1,353 · cited 2× · see citing works
“Only the strongest bands are listed in Table 1, or 724 – 1174 Couples with adjacent CH 2 groups, in phase mode at 724 cm − 1 most intense [79] Extended and corrected version of a previous compilation [150].”
BackgroundSelf-citation
Fourier Self-Deconvolution: A Method for Resolving Intrinsically Overlapped Bands
Kauppinen, J. K., Moffatt, D. J., Mantsch, H. H., & Cameron, D. G. (1981) · Applied Spectroscopy · doi:10.1366/0003702814732634 · Cited by 1,301 · cited 1× · see citing works
“…structure are: (i) fitting the amide I band with component bands [10,220,228] after identifying their position with band narrowing techniques [229 – 232] and (ii) decomposing the amide I band into basis spectra which have been calculated from a calibration set of spectra from proteins with…”
Method
Quantities, units and symbols in physical chemistry
Renner, T. (2007) · Royal Society of Chemistry eBooks · doi:10.1039/9781847557889 · Cited by 1,280 · see citing works
Structure of the Amide I Band of Peptides Measured by Femtosecond Nonlinear-Infrared Spectroscopy
Hamm, P. M., Lim, M., & Hochstrasser, R. M. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp9813286 · Cited by 1,107 · cited 1× · see citing works
“…effects: (i) Exciton transfer : if energy is absorbed by an oscillator it does not remain there but is rather transferred to a nearby oscillator with a typical time constant of 0.5 ps for an α - helix [178] — as a consequence the excited state is delocalised, typically over a length of 8 Å [178].”
BackgroundInfluential
The Chemical Bond in Inorganic Chemistry: The Bond Valence Model
Brown, I. D. (2002) · doi:10.1093/acprof:oso/9780198742951.001.0001 · Cited by 1,064 · cited 1× · see citing works
“This information has been evaluated [93] using a correlation between P \ O frequency and P \ O bond valence [100], the bond valence model [85,421] and empirical correlations to calculate P \ O bond strengths, P \ O bond lengths, and finally the dissociation energy of the bridging P \ O bond.”
Method
Redox-Coupled Crystal Structural Changes in Bovine Heart Cytochrome c Oxidase
Yoshikawa, S., Shinzawa‐Itoh, K., Nakashima, R., Yaono, R., Yamashita, E., Inoue, N., Yao, M., Fei, M. J., Libeu, C. P., Mizushima, T., et al. (1998) · Science · doi:10.1126/science.280.5370.1723 · Cited by 1,040 · cited 1× · see citing works
“The results are in line with the proposed role of this residue in proton pumping by mammalian oxidases [407].”
Result
Vibrational spectroscopy of water at the vapor/water interface
Du, Q., Superfine, R., Freysz, E., & Shen, Y. R. (1993) · Physical Review Letters · doi:10.1103/physrevlett.70.2313 · Cited by 1,036 · cited 1× · see citing works
“The symmetric and antisymmetric stretching vibrations of non-hydrogen bonded water absorb between 3630 and 3760 cm − 1 [274,277,292 – 296], whereas bonded OH groups absorb between 3600 and 2900 cm − 1 depending on the strength and pattern of hydrogen bonding [274,277,295].”
Background
Protein Hydration and Function
Rupley, J. A., & Careri, G. (1991) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60197-7 · Cited by 883 · cited 2× · see citing works
“Hydration of proteins has been studied by infrared spectroscopy as reviewed previously [276,278].”
Background
Quantitative studies of the structure of proteins in solution by fourier-transform infrared spectroscopy
Arrondo, J. L. R., Muga, A., Castresana, J., & Goñi, F. M. (1993) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(93)90006-6 · Cited by 866 · cited 2× · see citing works
“This makes infrared spectroscopy a valuable tool for the investigation of protein structure [1 – 11] of the molecular mechanism of protein reactions [2,10 – 35] and Further advantages of infrared spectroscopy are a large application range from small soluble proteins to large membrane proteins, a…”
BackgroundMethod
Anoxygenic photosynthetic bacteria
Knaff, D. B. (1996) · Photosynthesis Research · doi:10.1007/bf00016182 · Cited by 865 · see citing works
Infrared spectroscopy of biomolecules
Howland, J. L. (1996) · Biochemical Education · doi:10.1016/0307-4412(96)82531-3 · Cited by 799 · see citing works
Spectral Signatures of Hydrated Proton Vibrations in Water Clusters
Headrick, J. M., Diken, E. G., Walters, R. S., Hammer, N. I., Christie, R. A., Cui, J. X., Myshakin, E. M., Duncan, M. A., Johnson, M. A., & Jordan, K. D. (2005) · Science · doi:10.1126/science.1113094 · Cited by 797 · cited 2× · see citing works
“Protonated water clusters give rise to a particular absorption spectrum that depends critically on the number of water molecules over which the proton is delocalised [297].”
Background
Rapid photolytic release of adenosine 5'-triphosphate from a protected analog: utilization by the sodium:potassium pump of human red blood cell ghosts
Kaplan, J. H., Forbush, B., & Hoffman, J. F. (1978) · Biochemistry · doi:10.1021/bi00603a020 · Cited by 777 · see citing works
Photosynthetic Reaction Center
(1993) · Elsevier eBooks · doi:10.1016/c2009-0-02600-2 · Cited by 750 · see citing works
Chemical and steric constraints in inorganic solids
Brown, I. D. (1992) · Acta Crystallographica Section B Structural Science · doi:10.1107/s0108768192002453 · Cited by 718 · see citing works
[13] Resolution-enhanced fourier transform infrared spectroscopy of enzymes
Susi, H., & Byler, D. M. (1986) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(86)30015-6 · Cited by 706 · see citing works
Infrared spectroscopy of proteins and peptides in lipid bilayers
Tamm, L. K., & Tatulian, S. A. (1997) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583597003375 · Cited by 693 · cited 1× · see citing works
“The attenuated total reflectance (ATR) technique [26,124 – 126] is illustrated in Fig.”
Method
Infrared Spectroscopy of Size-Selected Water and Methanol Clusters
Buck, U., & Huisken, F. (2000) · Chemical Reviews · doi:10.1021/cr990054v · Cited by 667 · cited 2× · see citing works
“Infrared spectroscopy of liquid water [274 – 276] and water clusters [277] has been reviewed recently.”
Background
Infrared spectroscopy of biomolecules
Mantsch, H. H., & Chapman, D. (1996) · Cited by 608 · see citing works
Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. I. Spectral parameters of amino acid residue absorption bands
Venyaminov, S. Y., & Kalnin, N. N. (1990) · Biopolymers · doi:10.1002/bip.360301309 · Cited by 590 · cited 8× · see citing works
“…[79], Arg, Asn [152,154,155,424], Asp [152,154,155,432,433], Cys [434], Gln [152,154,155,435], Glu [154,155,432,433], His − [65,426], HisH [65,154,426], HisH 2+ [64,65,155], Lys [152,154,427], Phe [154], Pro [429,436,437], Ser [79,434,438,439], Thr [79,438], Trp, [162,430,440,441], Tyr…”
BackgroundInfluential
Spectroscopic Studies of the Hydrogen Bond. II. The Shift of the O–H Vibrational Frequency in the Formation of the Hydrogen Bond
Badger, R. M., & Bauer, S. H. (1937) · The Journal of Chemical Physics · doi:10.1063/1.1749952 · Cited by 582 · cited 1× · see citing works
“For the quantitative evaluation of band shifts induced by hydrogen bonding Badger and Bauer relationships [108] are often used.”
Method
Fast Events in Protein Folding: Helix Melting and Formation in a Small Peptide
Williams, S., Causgrove, T. P., Gilmanshin, R., Fang, K. S., Callender, R. H., Woodruff, W. H., & Dyer, R. B. (1996) · Biochemistry · doi:10.1021/bi952217p · Cited by 555 · cited 1× · see citing works
“…a cuvette that is held at a different temperature (time resolution 100 ms) [241,243], by a laser pulse near 2 μ m that is absorbed by the sample solvent 2 H 2 O [40,43,324,325] (temperature maximum reached after 20 ns [43]) or by a visible laser pulse that excites a heat transducing dye [326,327].”
Background
Infrared and Raman Spectroscopy of Biological Materials
Gremlich, H., & Yan, B. (2000) · CRC Press eBooks · doi:10.1201/b16936 · Cited by 534 · see citing works
Functional waters in intraprotein proton transfer monitored by FTIR difference spectroscopy
Garczarek, F., & Gerwert, K. B. (2005) · Nature · doi:10.1038/nature04231 · Cited by 533 · see citing works
Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes.
Goormaghtigh, E., Raussens, V., & Ruysschaert, J. (1999) · Biochimica et Biophysica Acta · doi:10.1016/s0304-4157(99)00004-0 · Cited by 531 · cited 2× · see citing works
“For protein samples, usually a protein film is prepared on the crystal surface [121,125,127,128], often simply by drying, and a buffer is placed on top of the film.”
Background
Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
Braiman, M. S., Mogi, T., Marti, T., Stern, L. J., Khorana, H. G., & Rothschild, K. J. (1988) · Biochemistry · doi:10.1021/bi00423a002 · Cited by 491 · cited 1× · see citing works
“Its proton is transferred to Asp-85 upon formation of the M intermediate [380,385,387,396] as identified by mutation of this residue [385,387].”
Background
Estimation of amino acid residue side‐chain absorption in the infrared spectra of protein solutions in heavy water
Chirgadze, Y. N., Fedorov, O., & Trushina, N. P. (1975) · Biopolymers · doi:10.1002/bip.1975.360140402 · Cited by 480 · cited 6× · see citing works
“…vibration References: aliphatic groups [79], Arg, Asn [152,154,155,424], Asp [152,154,155,432,433], Cys [434], Gln [152,154,155,435], Glu [154,155,432,433], His − [65,426], HisH [65,154,426], HisH 2+ [64,65,155], Lys [152,154,427], Phe [154], Pro [429,436,437], Ser [79,434,438,439], Thr…”
BackgroundInfluential
Correlation between the Vibrational Frequencies of the Carboxylate Group and the Types of Its Coordination to a Metal Ion: An ab Initio Molecular Orbital Study
Nara, M., Torii, H., & Tasumi, M. (1996) · The Journal of Physical Chemistry · doi:10.1021/jp9615924 · Cited by 463 · see citing works
FT-INFRARED AND FT-RAMAN SPECTROSCOPY IN BIOMEDICAL RESEARCH
Naumann, D. (2001) · Applied Spectroscopy Reviews · doi:10.1081/asr-100106157 · Cited by 463 · cited 1× · see citing works
“A striking example is the possibility to identify bacterial strains from the infrared spectrum and to differentiate and classify microorganisms [45].”
Background
Model calculations on the amide-I infrared bands of globular proteins
Torii, H., & Tasumi, M. (1992) · The Journal of Chemical Physics · doi:10.1063/1.461939 · Cited by 453 · see citing works
Crystal structure of the calcium pump with a bound ATP analogue
Toyoshima, C., & Mizutani, T. (2004) · Nature · doi:10.1038/nature02680 · Cited by 444 · cited 1× · see citing works
“This has later been confirmed by X-ray crystallography [417,418].”
Result
Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy
Goormaghtigh, E., Cabiaux, V., & Ruysschaert, J. (1994) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4615-1863-1_8 · Cited by 431 · cited 2× · see citing works
“The table is based on the experimental data and assignments of various authors collected and evaluated by Goormaghtigh et al. [6].”
BackgroundMethod
Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods
Dousseau, F., & Pézolet, M. (1990) · Biochemistry · doi:10.1021/bi00489a038 · Cited by 426 · see citing works
Phosphoryl Transfer and Calcium Ion Occlusion in the Calcium Pump
Sørensen, T. L.-M., MØLLER, J. V., & Nissen, P. (2004) · Science · doi:10.1126/science.1099366 · Cited by 426 · cited 1× · see citing works
“This has later been confirmed by X-ray crystallography [417,418].”
Result
Structure and dynamics of membrane proteins as studied by infrared spectroscopy
Arrondo, J. L. R., & Goñi, F. M. (1999) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(99)00007-3 · Cited by 425 · cited 1× · see citing works
“[36–38,43,44,241–246] and the topic has been reviewed [7,43,244].”
Biophysical Techniques in Photosynthesis
Amesz, J., & Hoff, A. J. (1996) · Advances in photosynthesis and respiration · doi:10.1007/0-306-47960-5 · Cited by 424 · see citing works
Evaluation of the Information Content in Infrared Spectra for Protein Secondary Structure Determination
Goormaghtigh, E., Ruysschaert, J., & Raussens, V. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.072017 · Cited by 423 · cited 1× · see citing works
“The error can be slightly reduced, and a prediction of the 3 10 -helix content included, by using three, but not more, wavenumbers specifically for each secondary structure [240].”
Background
Gas-Phase Infrared Spectrum of the Protonated Water Dimer
Asmis, K. R., Pivonka, N. L., Santambrogio, G., Brümmer, M., Kaposta, C., Neumark, D. M., & Wöste, L. H. (2003) · Science · doi:10.1126/science.1081634 · Cited by 416 · cited 1× · see citing works
“In particular, the isolated (i.e. non-solvated) Eigen cation H 3 O + (H 2 O) 3 has a characteristic absorption at 2665 cm − 1 (OH stretch) [297,298] and the isolated Zundel cation H 2 O ⋯ H + ⋯ OH 2 near 1750 cm − 1 (HOH bend) and 1050 cm − 1 (O ⋯ H + ⋯ O stretch or bend) [297,299].”
Background
Infrared Spectra and Protein Conformations in Aqueous Solutions
Susi, H., Timasheff, S. N., & Stevens, L. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99381-6 · Cited by 415 · see citing works
Water (H2O and D2O) Molar Absorptivity in the 1000–4000 cm−1Range and Quantitative Infrared Spectroscopy of Aqueous Solutions
Venyaminov, S. Y., & Prendergast, F. G. (1997) · Analytical Biochemistry · doi:10.1006/abio.1997.2136 · Cited by 409 · cited 2× · see citing works
“One drawback of infrared spectroscopy of aqueous solutions is the strong absorbance of water in the mid-infrared spectral region (near 1645 cm − 1 ) [120] which overlaps the important amide I band of proteins and some side chain bands (see below).”
Background
Internal Reflection Spectroscopy
Harrick, N. J., & Beckmann, K. H. (1974) · Springer eBooks · doi:10.1007/978-1-4613-4490-2_11 · Cited by 397 · see citing works
Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide
Lansbury, P. T., Costa, P. R., Griffiths, J. M., Simon, E. J., Auger, M., Halverson, K. J., Kocisko, D. A., Hendsch, Z. S., Ashburn, T. T., Spencer, R. G. S., et al. (1995) · Nature Structural & Molecular Biology · doi:10.1038/nsb1195-990 · Cited by 396 · cited 1× · see citing works
“This can be used to separate the amide I bands of two proteins or a protein and a peptide for binding studies [369,370], to probe the local secondary structure of peptides [188,211,371 – 375] or to determine band shifts due to hydrogen bonding to water [194,195].”
Method
The two-dimensional IR nonlinear spectroscopy of a cyclic penta-peptide in relation to its three-dimensional structure
Hamm, P. M., Lim, M., DeGrado, W. F., & Hochstrasser, R. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.5.2036 · Cited by 395 · cited 1× · see citing works
“There is evidence for some through-bond coupling between nearest neighbours from ab initio calculations on NMA [184] and di-and tripeptides [185 – 187] and from semiempirical calculations on larger peptides [188].”
Background
Properties and Uses of Photoreactive Caged Compounds
McCray, J. A., & Trentham, D. R. (1989) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.18.060189.001323 · Cited by 391 · see citing works
Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy
Goormaghtigh, E., Cabiaux, V., & Ruysschaert, J. (1994) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4615-1863-1_10 · Cited by 377 · see citing works
Laser-excited Raman spectroscopy of biomolecules
Lord, R. C., & Yu, N.-T. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90208-1 · Cited by 366 · see citing works
Identification of β-turn and random coil amide III infrared bands for secondary structure estimation of proteins
Cai, S., & Singh, B. R. (1999) · Biophysical Chemistry · doi:10.1016/s0301-4622(99)00060-5 · Cited by 360 · see citing works
Role of aspartate-96 in proton translocation by bacteriorhodopsin.
Gerwert, K. B., Hess, B., Soppa, J., & Oesterhelt, D. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.13.4943 · Cited by 350 · see citing works
Dynamic Studies in Biology
(2005) · Wiley eBooks · doi:10.1002/3527605592 · Cited by 321 · see citing works
Intermolecular Interaction Effects in the Amide I Vibrations of β Polypeptides
Krimm, S., & Abe, Y. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.10.2788 · Cited by 318 · cited 3× · see citing works
“This simple approach can explain the general features of amide I absorbance of secondary structures [173 – 176 (ii) For calculating the amide I band of proteins, a “ floating oscillator model ” has been developed [203,204].”
Background
A Distinct Utility of the Amide III Infrared Band for Secondary Structure Estimation of Aqueous Protein Solutions Using Partial Least Squares Methods
Cai, S., & Singh, B. R. (2004) · Biochemistry · doi:10.1021/bi030149y · Cited by 313 · cited 1× · see citing works
“In spite of side chain contributions to the amide III mode, this mode can be used for secondary structure prediction [166 – 169].”
Method
Infrared spectra and resonance interaction of amide‐I vibration of the antiparallel‐chain pleated sheet
Chirgadze, Y. N., & Nevskaya, N. A. (1976) · Biopolymers · doi:10.1002/bip.1976.360150402 · Cited by 312 · cited 7× · see citing works
“This simple approach can explain the general features of amide I absorbance of secondary structures [173 – 176 (ii) For calculating the amide I band of proteins, a “ floating oscillator model ” has been developed [203,204].”
BackgroundInfluential
Differentiation of β-Sheet-Forming Structures: Ab Initio-Based Simulations of IR Absorption and Vibrational CD for Model Peptide and Protein β-Sheets
Kubelka, J., & Keiderling, T. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja0116627 · Cited by 306 · cited 4× · see citing works
“However, as discussed above, similar spectra are expected for finite or twisted β -sheets [175,176,203,212] and there is no experimental evidence for a difference between the frequencies of parallel and antiparallel β -sheet [218,220].”
BackgroundInfluential
Infrared spectra and molar absorption coefficients of the 20 alpha amino acids in aqueous solutions in the spectral range from 1800 to 500cm−1
Wolpert, M., & Hellwig, P. (2006) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2005.08.025 · Cited by 301 · cited 1× · see citing works
“Table 1 gives an overview of the infrared absorption of amino acid side chains in 1 H 2 O and 2 H 2 O [11,150], see also further compilations of infrared bands [4,151 – 156] and of Raman bands [157 – 162].”
Background
Light-driven protonation changes of internal aspartic acids of bacteriorhodopsin: an investigation of static and time-resolved infrared difference spectroscopy using [4-13C]aspartic acid labeled purple membrane
Engelhard, M., Gerwert, K. B., Hess, B., & Siebert, F. (1985) · Biochemistry · doi:10.1021/bi00323a024 · Cited by 297 · cited 1× · see citing works
“…importance was the identification of the proton transporting groups from the early detection of protonated carboxyl groups [376,378] to the assignment to specific residues or a localised protonated water cluster using isotopic labeling [384 – 386] and site-directed mutagenesis [307,385 – 388].”
Background
Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. II. Amide absorption bands of polypeptides and fibrous proteins in α‐, β‐, and random coil conformations
Venyaminov, S. Y., & Kalnin, N. N. (1990) · Biopolymers · doi:10.1002/bip.360301310 · Cited by 294 · cited 2× · see citing works
“The result is a splitting of the amide I band, which can be as large as ∼ 70 cm − 1 [179,180] for β -sheet structures.”
Background
FTIR difference spectroscopy of bacteriorhodopsin: Toward a molecular model
Rothschild, K. J. (1992) · Journal of Bioenergetics and Biomembranes · doi:10.1007/bf00762674 · Cited by 292 · cited 3× · see citing works
“Here, continuous illumination or a light flash induces a reaction in photosensitive proteins like bacteriorhodopsin [14 – 17] or photosynthetic reaction centers [12,13,21,22].”
Background
The effect of cooperative hydrogen bonding on the OH stretching-band shift for water clusters studied by matrix-isolation infrared spectroscopy and density functional theory
Ohno, K., Okimura, M., Akai, N., & Katsumoto, Y. (2005) · Physical Chemistry Chemical Physics · doi:10.1039/b506641g · Cited by 292 · cited 1× · see citing works
“The symmetric and antisymmetric stretching vibrations of non-hydrogen bonded water absorb between 3630 and 3760 cm − 1 [274,277,292 – 296], whereas bonded OH groups absorb between 3600 and 2900 cm − 1 depending on the strength and pattern of hydrogen bonding [274,277,295].”
Background
A decade of vibrational micro-spectroscopy of human cells and tissue (1994–2004)
Diem, M., Romeo, M., Boydston‐White, S., Miljković, M. D., & Matthäus, C. (2004) · The Analyst · doi:10.1039/b408952a · Cited by 290 · see citing works
Infrared spectra and resonance interactions of amide‐I and II vibrations of α‐helix
Nevskaya, N. A., & Chirgadze, Y. N. (1976) · Biopolymers · doi:10.1002/bip.1976.360150404 · Cited by 280 · cited 4× · see citing works
“Nevertheless it has led to interesting insight [29,174 – 176,203 , 204 ,206 ] (iii) A normal mode analysis can be carried out using a simplified general valence force field for the polypeptide with that of N -methylacetamide serving as a starting point [151].”
BackgroundInfluential
Ab initio molecular orbital study of the amide I vibrational interactions between the peptide groups in di- and tripeptides and considerations on the conformation of the extended helix
Torii, H., & Tasumi, M. (1998) · Journal of Raman Spectroscopy · doi:10.1002/(sici)1097-4555(199801)29:1 · Cited by 275 · see citing works
FT-IR Characterization of Metal Acetates in Aqueous Solution
Tackett, J. E. (1989) · Applied Spectroscopy · doi:10.1366/0003702894202931 · Cited by 271 · cited 2× · see citing works
“In deuterated proteins up to 10 cm lower [155,424] HisH2 , ν(C_C) 1631 (250) 1600 (35), 1623 (16) Only one strong band observed for 4-methylimidazole at 1633 (H2O) and 1605 cm −1 ((2)H2O) [426] Lys, δas(NH3 ) 1626–1629 (60–130) 1201 (2)H2O band position based on shift observed for CH3NH3Cl and CH3N (2)H3Cl Tyr-OH, ν(C…”
Background
Redox‐linked conformational changes in proteins detected by a combination of infrared spectroscopy and protein electrochemistry
Moss, D. A., Nabedryk, E., Breton, J., & Mäntele, W. (1990) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1990.tb15338.x · Cited by 270 · cited 1× · see citing works
“Infrared investigations became available with the development of an ultra-thin-layer spectroelectrochemical cell suitable for protein investigations in aqueous solution [330].”
Background
Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy.
Gerwert, K. B., Souvignier, G., & Hess, B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.24.9774 · Cited by 268 · cited 2× · see citing works
“Its proton is transferred to Asp-85 upon formation of the M intermediate [380,385,387,396] as identified by mutation of this residue [385,387].”
Background
Determination of protein secondary structure using factor analysis of infrared spectra
Lee, D. C., Haris, P. I., Chapman, D., & Mitchell, R. C. (1990) · Biochemistry · doi:10.1021/bi00491a012 · Cited by 266 · see citing works
A Genetically Encoded Infrared Probe
Schultz, K. C., Supeková, Ľ., Ryu, Y., Xie, J., Perera, R., & Schultz, P. G. (2006) · Journal of the American Chemical Society · doi:10.1021/ja0636690 · Cited by 265 · cited 1× · see citing works
“This notion of infrared spectroscopy being a marker-free technique has recently received an interesting twist in a study that reported a genetically encoded CN infrared label which was used to probe ligand binding to myoglobin [50].”
Background
Beware of proteins in DMSO
Jackson, M., & Mantsch, H. H. (1991) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/0167-4838(91)90563-f · Cited by 264 · see citing works
Structural characterization of the pressure-denatured state and unfolding/refolding kinetics of staphylococcal nuclease by synchrotron small-angle X-ray scattering and Fourier-transform infrared spectroscopy 1 1Edited by P. E. Wright
Panick, G., Malessa, R., Winter, R., Rapp, G., Frye, K. J., & Royer, C. A. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1454 · Cited by 263 · cited 1× · see citing works
“Pressure-jump experiments [328,329] require a cell that allows to set the sample under pressures of several kbar and have an experimental dead time of about 20 s. Equilibrium electrochemistry can be used to initiate redox reactions of proteins.”
Method
Two-dimensional infrared spectroscopy: a promising new method for the time resolution of structures
Zanni, M. T., & Hochstrasser, R. M. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00243-8 · Cited by 253 · cited 1× · see citing works
“All techniques mentioned and biological or photochemical applications thereof have been reviewed before [20,23,133 – 143].”
Method
Ultrafast vibrational spectroscopy of water and aqueous N-methylacetamide: Comparison of different electronic structure/molecular dynamics approaches
Schmidt, J. R., Corcelli, S. A., & Skinner, J. L. (2004) · The Journal of Chemical Physics · doi:10.1063/1.1791632 · Cited by 251 · cited 3× · see citing works
“The models differ as to whether the electric effects of the environment on a given amide group are accounted for by the electric potential [197 – 199], the electric field [200], or a combination of electric field and its derivatives [113,201].”
BackgroundResult
Biochemical applications of surface-enhanced infrared absorption spectroscopy
Ataka, K., & Heberle, J. (2007) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-006-1071-4 · Cited by 250 · cited 1× · see citing works
“A promising technique to further reduce the amount of material is surface-enhanced infrared spectroscopy [123] — the infrared analog of surface enhanced Raman spectroscopy.”
Method
Time-Resolved FT-IR Absorption Spectroscopy Using a Step-Scan Interferometer
Uhmann, W., Becker, A., Taran, C., & Siebert, F. (1991) · Applied Spectroscopy · doi:10.1366/0003702914337128 · Cited by 246 · cited 2× · see citing works
“…made it possible to apply time-resolved techniques like single wavelength measurements with a global source [377 – 379], stroboscopic FTIR spectroscopy [380,381] and the step scan technique [144,382,383] which require numerous repetitions of the flash-induced experiment on a single sample.”
BackgroundMethod
Two-dimensional heterodyned and stimulated infrared photon echoes of N-methylacetamide-D
Zanni, M. T., Asplund, M. C., & Hochstrasser, R. M. (2001) · The Journal of Chemical Physics · doi:10.1063/1.1346647 · Cited by 245 · cited 1× · see citing works
“Motional narrowing can counteract the effects of a heterogeneous environment for amide groups that are hydrogen bonded to bulk water [111 – 113].”
Background
Insight into protein structure and protein-ligand recognition by Fourier transform infrared spectroscopy
Jung, C. (2000) · Journal of Molecular Recognition · doi:10.1002/1099-1352(200011/12)13:6 · Cited by 245 · see citing works
Correlation between electronic and molecular structure distortions and vibrational properties. II. Amide I modes of NMA–nD2O complexes
Ham, S., Kim, J.-H., Lee, H., & Cho, M. (2003) · The Journal of Chemical Physics · doi:10.1063/1.1536980 · Cited by 242 · cited 2× · see citing works
“The models differ as to whether the electric effects of the environment on a given amide group are accounted for by the electric potential [197 – 199], the electric field [200], or a combination of electric field and its derivatives [113,201].”
Background
UV Resonance Raman excitation profiles of the aromatic amino acids
Asher, S. A., Ludwig, M. J., & Johnson, C. R. (1986) · Journal of the American Chemical Society · doi:10.1021/ja00272a005 · Cited by 241 · see citing works
Infrared Spectra of Amide Groups in α-Helical Proteins: Evidence for Hydrogen Bonding between Helices and Water
Manas, E. S., Getahun, Z., Wright, W. W., DeGrado, W. F., & Vanderkooi, J. M. (2000) · Journal of the American Chemical Society · doi:10.1021/ja001782z · Cited by 238 · cited 1× · see citing works
“This can be used to separate the amide I bands of two proteins or a protein and a peptide for binding studies [369,370], to probe the local secondary structure of peptides [188,211,371 – 375] or to determine band shifts due to hydrogen bonding to water [194,195].”
Method
A transferable electrostatic map for solvation effects on amide I vibrations and its application to linear and two-dimensional spectroscopy
Jansen, T. L. C., & Knoester, J. (2006) · The Journal of Chemical Physics · doi:10.1063/1.2148409 · Cited by 238 · cited 3× · see citing works
“Motional narrowing can counteract the effects of a heterogeneous environment for amide groups that are hydrogen bonded to bulk water [111 – 113].”
Background
Role of internal water molecules in bacteriorhodopsin
Kandori, H. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00138-9 · Cited by 236 · see citing works
A new approach to time-resolved studies of ATP-requiring biological systems; laser flash photolysis of caged ATP.
McCray, J. A., Herbette, L. G., Kihara, T., & Trentham, D. R. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.12.7237 · Cited by 230 · see citing works
Elucidation of Residue-Level Structure and Dynamics of Polypeptides via Isotope-Edited Infrared Spectroscopy
Decatur, S. M. (2006) · Accounts of Chemical Research · doi:10.1021/ar050135f · Cited by 230 · see citing works
Normal vibrations of crystalline polyglycine I
Abe, Y., & Krimm, S. (1972) · Biopolymers · doi:10.1002/bip.1972.360110905 · Cited by 223 · cited 3× · see citing works
“Only with the introduction of the transition dipole coupling mechanism [170] this splitting in a main band near 1630 cm − 1 and a side band near 1690 cm − 1 could be explained.”
Background
.beta.-Lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin
Fisher, J. F., Belasco, J. G., Khosla, S., & Knowles, J. R. (1980) · Biochemistry · doi:10.1021/bi00554a012 · Cited by 221 · cited 1× · see citing works
“Examples for infrared spectroscopic measurements of enzyme activity are cefoxitin hydrolysis by β -lactamase [77], deacylation of cinnamoyl-chymotrypsin [78], ATP hydrolysis by the Ca 2+ - ATPase [72], oxidation of D -glucose by glucose oxidase [74], hydrolysis of amides [76,273], synthesis of…”
Method
Modeling the amide I bands of small peptides
Jansen, T. L. C., Dijkstra, A. G., Watson, T. M., Hirst, J. D., & Knoester, J. (2006) · The Journal of Chemical Physics · doi:10.1063/1.2218516 · Cited by 219 · cited 2× · see citing works
“Several of the approaches have been compared and shown to yield similar results for NMA in water ( 2 H 2 O) [200], but for the intramolecular interaction within small peptides, the correlation between frequency and electric potential works best [196].”
BackgroundResult
The vibrational spectrum of the hydrated proton: Comparison of experiment, simulation, and normal mode analysis
Kim, J., Schmitt, U. W., Gruetzmacher, J. A., Voth, G. A., & Scherer, N. E. (2002) · The Journal of Chemical Physics · doi:10.1063/1.1423327 · Cited by 214 · cited 1× · see citing works
“An acidic aqueous solution exhibits a broad continuous absorption between 1000 and 3100 cm − 1 and additional bands with respect to neutral water near 1200, 1740, and 2900 cm − 1 [269,300 – 303] consistent with the presence of both, the Eigen and the Zundel forms of the hydrated proton [303].”
Background
Occurrence and Characteristics of a Rapid Exchange of Phosphate Oxygens Catalyzed by Sarcoplasmic Reticulum Vesicles
Kanazawa, T., & Boyer, P. D. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)44022-2 · Cited by 209 · see citing works
Regulation of β-Sheet Structures within Amyloid-Like β-Sheet Assemblage from Tripeptide Derivatives
Yamada, N., Ariga, K., Naito, M., Matsubara, K., & Koyama, E. (1998) · Journal of the American Chemical Society · doi:10.1021/ja981363q · Cited by 209 · cited 1× · see citing works
“In consequence, the high-wavenumber side band is often, but not always, absent for parallel β -sheets [217 – 219].”
Background
Hydrogen Bonds with Large Proton Polarizability and Proton Transfer Processes in Electrochemistry and Biology
Zuńdel, G. (1999) · Advances in chemical physics · doi:10.1002/9780470141700.ch1 · Cited by 202 · cited 1× · see citing works
“An acidic aqueous solution exhibits a broad continuous absorption between 1000 and 3100 cm − 1 and additional bands with respect to neutral water near 1200, 1740, and 2900 cm − 1 [269,300 – 303] consistent with the presence of both, the Eigen and the Zundel forms of the hydrated proton [303].”
Background
Laser-excited Raman spectroscopy of biomolecules
Lord, R. C., & Yu, N. (1970) · Journal of Molecular Biology · doi:10.1016/0022-2836(70)90137-3 · Cited by 201 · cited 1× · see citing works
“Table 1 gives an overview of the infrared absorption of amino acid side chains in 1 H 2 O and 2 H 2 O [11,150], see also further compilations of infrared bands [4,151 – 156] and of Raman bands [157 – 162].”
Background
Proton binding within a membrane protein by a protonated water cluster
Garczarek, F., Brown, L. S., Lanyi, J. Κ., & Gerwert, K. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0500421102 · Cited by 201 · cited 5× · see citing works
“Infrared spectroscopy has detected protonated water clusters in proteins, for example in a bacterial reaction centre [302] and in bacteriorhodopsin [304 – 307], where the localisation of the proton is affected by mutation of nearby amino acids [307].”
BackgroundMethodInfluential
Membrane binding induces destabilization of cytochrome c structure
Muga, A., Mantsch, H. H., & Surewicz, W. K. (1991) · Biochemistry · doi:10.1021/bi00243a025 · Cited by 200 · cited 1× · see citing works
“The exchange characteristics of proteins might depend on their particular physiological state and can be modulated by the binding of ligands [257,258], during catalysis [259] or by interaction with membranes [260].”
Background
Resonance enhancement in the ultraviolet Raman spectra of aromatic amino acids
Rava, R. P., & Spiro, T. G. (1985) · The Journal of Physical Chemistry · doi:10.1021/j100256a007 · Cited by 200 · see citing works
Ab Initio Calculation of Amide Carbonyl Stretch Vibrational Frequencies in Solution with Modified Basis Sets. 1. N-Methyl Acetamide
Kubelka, J., & Keiderling, T. A. (2001) · The Journal of Physical Chemistry A · doi:10.1021/jp013203y · Cited by 198 · cited 3× · see citing works
“The combination of explicit water molecules in the first hydration shell and of a continuum model for water reproduces the experimentally observed shifts [190,191].”
BackgroundMethod
Infrared Spectroscopy of Proteins
Fabian, H., & Mäntele, W. (2001) · Handbook of Vibrational Spectroscopy · doi:10.1002/0470027320.s8201 · Cited by 195 · cited 5× · see citing works
“Instead, the protein reaction of interest has to be initiated directly in the cuvette and the associated infrared absorbance changes can be recorded [2,10,20,23,135].”
BackgroundMethodInfluential
Empirical modeling of the peptide amide I band IR intensity in water solution
Bouř, P., & Keiderling, T. A. (2003) · The Journal of Chemical Physics · doi:10.1063/1.1622384 · Cited by 195 · cited 2× · see citing works
“The models differ as to whether the electric effects of the environment on a given amide group are accounted for by the electric potential [197 – 199], the electric field [200], or a combination of electric field and its derivatives [113,201].”
Background
Bacteriorhodopsin's Intramolecular Proton-Release Pathway Consists of a Hydrogen-Bonded Network
Rammelsberg, R., Huhn, G., Lübben, M., & Gerwert, K. B. (1998) · Biochemistry · doi:10.1021/bi971701k · Cited by 193 · see citing works
Secondary Structure Estimation of Proteins Using the Amide III Region of Fourier Transform Infrared Spectroscopy: Application to Analyze Calcium-Binding-Induced Structural Changes in Calsequestrin
Fu, F.-N., DeOliveira, D. B., Trumble, W. R., Sarkar, H. K., & Singh, B. R. (1994) · Applied Spectroscopy · doi:10.1366/0003702944028065 · Cited by 191 · see citing works
Vibrational Spectra and Ab Initio DFT Calculations of 4-Methylimidazole and Its Different Protonation Forms: Infrared and Raman Markers of the Protonation State of a Histidine Side Chain
Hasegawa, K., Ono, T.-A., & Noguchi, T. (2000) · The Journal of Physical Chemistry B · doi:10.1021/jp000157d · Cited by 188 · cited 2× · see citing works
“…aliphatic groups [79], Arg, Asn [152,154,155,424], Asp [152,154,155,432,433], Cys [434], Gln [152,154,155,435], Glu [154,155,432,433], His − [65,426], HisH [65,154,426], HisH 2+ [64,65,155], Lys [152,154,427], Phe [154], Pro [429,436,437], Ser [79,434,438,439], Thr [79,438], Trp,…”
Background
Does Fourier-transform infrared spectroscopy provide useful information on protein structures?
Haris, P. I., & Chapman, D. (1992) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(92)90305-s · Cited by 187 · cited 1× · see citing works
“Probably the most common application of infrared spectroscopy in protein studies is the analysis of secondary structure [1,3,4,6,8 – 10, 221, 222 ].”
Background
The optimization of protein secondary structure determination with infrared and circular dichroism spectra
Oberg, K. A., Ruysschaert, J., & Goormaghtigh, E. (2004) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.2004.04220.x · Cited by 185 · cited 1× · see citing works
“Nevertheless it provides valuable structural information and secondary structure prediction can be done with the amide II band alone [165].”
Background
Infrared Studies of Fast Events in Protein Folding
Dyer, R. B., Gai, F., Woodruff, W. H., Gilmanshin, R., & Callender, R. H. (1998) · Accounts of Chemical Research · doi:10.1021/ar970343a · Cited by 185 · see citing works
Ultrafast thermally induced unfolding of RNase A.
Phillips, C. M., Mizutani, Y., & Hochstrasser, R. M. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.16.7292 · Cited by 184 · cited 1× · see citing works
“…a cuvette that is held at a different temperature (time resolution 100 ms) [241,243], by a laser pulse near 2 μ m that is absorbed by the sample solvent 2 H 2 O [40,43,324,325] (temperature maximum reached after 20 ns [43]) or by a visible laser pulse that excites a heat transducing dye [326,327].”
Background
Infrared Spectra and Protein Conformations in Aqueous Solutions
Timasheff, S. N., Susi, H., & Stevens, L. (1967) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)99382-8 · Cited by 183 · cited 1× · see citing works
“Probably the most common application of infrared spectroscopy in protein studies is the analysis of secondary structure [1,3,4,6,8 – 10, 221, 222 ].”
Background
Infrared spectra of labelled compounds
Pinchas, S., & Laulicht, I. (1971) · Medical Entomology and Zoology · Cited by 182 · see citing works
Infrared study of bound carbon monoxide in the human red blood cell, isolated hemoglobin, and heme carbonyls
Alben, J. O., & Caughey, W. S. (1968) · Biochemistry · doi:10.1021/bi00841a022 · Cited by 182 · cited 3× · see citing works
“This has been done by carefully subtracting the spectrum of a sample where the protein is in state B from a spectrum where it is in state A [262,264 – 271].”
BackgroundMethod
Reaction-induced infrared difference spectroscopy for the study of protein function and reaction mechanisms
Mäntele, W. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90186-q · Cited by 182 · cited 2× · see citing works
“They have been reviewed before [2,14,15,18,20,24,25,27,28,30] and are only briefly discussed here.”
BackgroundMethod
Evidence for light‐induced 13‐cis, 14‐s‐cis isomerization in bacteriorhodopsin obtained by FTIR difference spectroscopy using isotopically labelled retinals
Gerwert, K. B., & Siebert, F. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04285.x · Cited by 180 · cited 1× · see citing works
“Protein cofactors have also been labeled for example for bacteriorho-dopsin [17,362], photosynthetic reaction centres [12,13,22] and cytochrome c oxidase [335].”
Background
Electrostatic DFT Map for the Complete Vibrational Amide Band of NMA
Hayashi, T., Zhuang, W., & Mukamel, S. (2005) · The Journal of Physical Chemistry A · doi:10.1021/jp052324l · Cited by 180 · cited 2× · see citing works
“The models differ as to whether the electric effects of the environment on a given amide group are accounted for by the electric potential [197 – 199], the electric field [200], or a combination of electric field and its derivatives [113,201].”
Background
Normal coordinate analysis of the indole ring
Takeuchi, H., & Harada, I. (1986) · Spectrochimica Acta Part A Molecular Spectroscopy · doi:10.1016/0584-8539(86)80021-6 · Cited by 179 · cited 2× · see citing works
“Vibrations dominated by amide group motions are not included. ν stretching vibration, ν s: symmetric stretching vibration, ν as : antisymmetric stretching vibration, δ : in plane bending vibration, δ as : asymmetric in plane bending vibration, γ w : wagging vibration, γ t : twisting vibration, γ r : rocking vibration…”
Background
Laser Raman Scattering as a Probe of Protein Structure
Spiro, T. G., & Gaber, B. P. (1977) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.46.070177.003005 · Cited by 177 · see citing works
Infrared spectroscopy of phosphatidylcholines in aqueous suspension a study of the phosphate group vibrations
Arrondo, J. L. R., Goñi, F. M., & Macarulla, J. M. (1984) · Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism · doi:10.1016/0005-2760(84)90310-2 · Cited by 177 · see citing works
In situ determination of transient pK a changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopy
Zscherp, C., Schlesinger, R., Tittor, J., Oesterhelt, D., & Heberle, J. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5498 · Cited by 174 · cited 2× · see citing works
“An example is Asp-96 of bacteriorhodopsin for which a p K a N 12 has been found [163].”
BackgroundInfluential
Bovine serum albumin observed by infrared spectrometry. I. Methodology, structural investigation, and water uptake
Grdadolnik, J., & Mar�chal, Y. (2000) · Biopolymers · doi:10.1002/1097-0282(2001)62:1 · Cited by 172 · see citing works
Proton transfer reactions across bacteriorhodopsin and along the membrane
Heberle, J. (2000) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/s0005-2728(00)00064-5 · Cited by 172 · see citing works
Protein secondary structure from fourier transform infrared spectroscopy: A data base analysis
Sarver, R. W., & Krueger, W. C. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90155-m · Cited by 171 · cited 1× · see citing works
“…the amide I band with component bands [10,220,228] after identifying their position with band narrowing techniques [229 – 232] and (ii) decomposing the amide I band into basis spectra which have been calculated from a calibration set of spectra from proteins with known structure [10,233 – 238].”
Method
Site-specific conformational determination in thermal unfolding studies of helical peptides using vibrational circular dichroism with isotopic substitution
Silva, R. A. G. D., Kubelka, J., Bouř, P., Decatur, S. M., & Keiderling, T. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.140161997 · Cited by 171 · see citing works
Sum-frequency spectroscopic studies of ice interfaces
Wei, X., Miranda, P. B., Zhang, C., & Shen, Y. R. (2002) · Physical review. B, Condensed matter · doi:10.1103/physrevb.66.085401 · Cited by 170 · see citing works
Electrochemical and infrared-spectroscopic characterization of redox reactions of p-quinones
Bauscher, M., & Maentele, W. (1992) · The Journal of Physical Chemistry · doi:10.1021/j100205a087 · Cited by 168 · see citing works
Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates.
Braiman, M. S., Bousché, O., & Rothschild, K. J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.6.2388 · Cited by 166 · cited 3× · see citing works
“Its proton is transferred to Asp-85 upon formation of the M intermediate [380,385,387,396] as identified by mutation of this residue [385,387].”
Background
A Quantitative Reconstruction of the Amide I Contour in the IR Spectra of Globular Proteins: From Structure to Spectrum
Brauner, J. W., Flach, C. R., & Mendelsohn, R. (2004) · Journal of the American Chemical Society · doi:10.1021/ja0400685 · Cited by 165 · see citing works
Bacteriorhodopsin — the movie
Kühlbrandt, W. (2000) · Nature · doi:10.1038/35020654 · Cited by 162 · cited 1× · see citing works
“Combining this knowledge from infrared spectroscopy with that from recent structures at atomic resolution “ the path of the proton through the membrane can now be followed in exquisite detail ” [389].”
Background
Intensities and other spectral parameters of infrared amide bands of polypeptides in the β‐ and random forms
Chirgadze, Y. N., Shestopalov, B. V., & Venyaminov, S. Y. (1973) · Biopolymers · doi:10.1002/bip.1973.360120610 · Cited by 159 · cited 1× · see citing works
“The result is a splitting of the amide I band, which can be as large as ∼ 70 cm − 1 [179,180] for β -sheet structures.”
Background
Structure of the I1 early intermediate of photoactive yellow protein by FTIR spectroscopy.
Brudler, R., Rammelsberg, R., Woo, T. T., Getzoff, E. D., & Gerwert, K. B. (2001) · Nature Structural Biology · doi:10.1038/85021 · Cited by 158 · cited 1× · see citing works
“This approach has been used in studies of the Ca 2+ -ATPase pump mechanism [349] of the photoactive yellow protein photocycle [350], and of protein folding studies [36,38,42,43].”
Method
Advances in vibrational spectroscopy as a sensitive probe of peptide and protein structure
Schweitzer‐Stenner, R. (2006) · Vibrational Spectroscopy · doi:10.1016/j.vibspec.2006.01.004 · Cited by 158 · cited 1× · see citing works
“The fundamental mechanism that renders the amide I vibration sensitive to secondary structure is transition dipole coupling (TDC) [170,173 – 177].”
Background
Transition dipole coupling in Amide I modes of βpolypeptides
Moore, W. H., & Krimm, S. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.12.4933 · Cited by 156 · see citing works
Involvement of Glutamic Acid 278 in the Redox Reaction of the Cytochrome c Oxidase from Paracoccus denitrificans Investigated by FTIR Spectroscopy
Hellwig, P., Behr, J., Ostermeier, C., Richter, O. H., Pfitzner, U., Odenwald, A., Ludwig, B., Michel, H., & Mäntele, W. (1998) · Biochemistry · doi:10.1021/bi9725576 · Cited by 156 · cited 3× · see citing works
“While much of the initial work has been on photosynthetic proteins (see references above), recent work has concentrated on cytochrome c oxidases [32,333 – 340].”
Background
Investigation of the Primary Photochemistry of Bacteriorhodopsin by Low‐Temperature Fourier‐Transform Infrared Spectroscopy
Siebert, F., & Mäntele, W. (1983) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1983.tb07187.x · Cited by 156 · cited 1× · see citing works
“The retinal Schiff base remains protonated in the early phase of the photocycle [391].”
Background
Optical methods in cell physiology
Ronot, X., & Adolphe, M. (1987) · Biochimie · doi:10.1016/0300-9084(87)90035-6 · Cited by 154 · see citing works
A survey of the plant mitochondrial proteome in relation to development
Bardel, J., Louwagie, M., Jaquinod, M., Jourdain, A., Luche, S., Rabilloud, T., Macherel, D., Garin, J., & Bourguignon, J. (2002) · PROTEOMICS · doi:10.1002/1615-9861(200207)2:7 · Cited by 153 · see citing works
Effects of Intermolecular Hydrogen-Bonding Interactions on the Amide I Mode of N-Methylacetamide: Matrix-Isolation Infrared Studies and ab Initio Molecular Orbital Calculations
Torii, H., Tatsumi, T., Kanazawa, T., & Tasumi, M. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp972879j · Cited by 153 · cited 1× · see citing works
“The effects of hydrogen bonding on the infrared spectrum of NMA have been examined computationally in ab initio calculations and experimentally [171,189 – 191].”
Method
Infrared spectra and resonance interaction of amide‐I vibration of the parallel‐chain pleated sheet
Chirgadze, Y. N., & Nevskaya, N. A. (1976) · Biopolymers · doi:10.1002/bip.1976.360150403 · Cited by 153 · cited 6× · see citing works
“Parallel β -sheets [173,175] have their main absorption at higher wavenumber than corresponding antiparallel β -sheets [173,176] although the difference can be as little as 4 cm − 1 [217] and the parallel β -sheet band can be as low as 1622 cm − 1 (in H 2 O) for β -barrel proteins [218] and as low…”
BackgroundInfluential
Spectra of dangling OH groups at ice cluster surfaces and within pores of amorphous ice
Rowland, B., & Devlin, J. P. (1991) · The Journal of Chemical Physics · doi:10.1063/1.460303 · Cited by 150 · see citing works
Conformational changes of bacteriorhodopsin detected by Fourier transform infrared difference spectroscopy
Rothschild, K. J., Zagaeski, M., & Cantore, W. A. (1981) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(81)90478-2 · Cited by 149 · cited 2× · see citing works
“Of particular importance was the identification of the proton transporting groups from the early detection of protonated carboxyl groups [376,378] to the assignment to specific residues or a localised protonated water cluster using isotopic labeling [384 – 386] and site-directed mutagenesis…”
Background
Quantitative IR spectrophotometry of peptide compounds in water (H2O) solutions. III. Estimation of the protein secondary structure
Kalnin, N. N., Baikalov, I., & Venyaminov, S. Y. (1990) · Biopolymers · doi:10.1002/bip.360301311 · Cited by 147 · see citing works
Cytochrome oxidase (a3) heme and copper observed by low-temperature Fourier transform infrared spectroscopy of the CO complex.
Alben, J. O., Moh, P. P., Fiamingo, F. G., & Altschuld, R. A. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.1.234 · Cited by 146 · cited 2× · see citing works
“Already in 1981, CO photodissociation experiments have led to significant conclusions regarding the catalytic centre [402].”
Background
The hydration of amides in helices; a comprehensive picture from molecular dynamics, IR, and NMR
Walsh, S. T. R., Cheng, R. P., Wright, W. W., Alonso, D. O. V., Daggett, V., Vanderkooi, J. M., & DeGrado, W. F. (2003) · Protein Science · doi:10.1110/ps.0223003 · Cited by 146 · cited 2× · see citing works
“This can be used to separate the amide I bands of two proteins or a protein and a peptide for binding studies [369,370], to probe the local secondary structure of peptides [188,211,371 – 375] or to determine band shifts due to hydrogen bonding to water [194,195].”
BackgroundMethod
Fourier transform infrared spectroscopic studies of calcium-binding proteins
Jackson, M., Haris, P. I., & Chapman, D. (1991) · Biochemistry · doi:10.1021/bi00104a016 · Cited by 146 · see citing works
Infrared spectroscopy: a new frontier in medicine
Jackson, M., Sowa, M. G., & Mantsch, H. H. (1997) · Biophysical Chemistry · doi:10.1016/s0301-4622(97)80555-8 · Cited by 145 · see citing works
Nature of Vibrational Coupling in Helical Peptides: An Isotopic Labeling Study
Huang, R., Kubelka, J., Barber-Armstrong, W., Silva, R. A. G. D., Decatur, S. M., & Keiderling, T. A. (2004) · Journal of the American Chemical Society · doi:10.1021/ja037998t · Cited by 144 · cited 1× · see citing works
“At short distances ( b 6 Å [181]) the TDC approximation becomes less satisfactory [181 – 183].”
Background
The Anomalous Infrared Amide I Intensity Distribution in 13C Isotopically Labeled Peptide β-Sheets Comes from Extended, Multiple-Stranded Structures. An ab Initio Study
Kubelka, J., & Keiderling, T. A. (2001) · Journal of the American Chemical Society · doi:10.1021/ja010270x · Cited by 142 · cited 3× · see citing works
“This can be used to separate the amide I bands of two proteins or a protein and a peptide for binding studies [369,370], to probe the local secondary structure of peptides [188,211,371 – 375] or to determine band shifts due to hydrogen bonding to water [194,195].”
BackgroundMethod
Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy
Goormaghtigh, E., Cabiaux, V., & Ruysschaert, J. (1994) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-1-4615-1863-1_9 · Cited by 141 · cited 2× · see citing works
“Table 1 gives an overview of the infrared absorption of amino acid side chains in 1 H 2 O and 2 H 2 O [11,150], see also further compilations of infrared bands [4,151 – 156] and of Raman bands [157 – 162].”
Background
13C Isotope Labeling of Hydrophobic Peptides. Origin of the Anomalous Intensity Distribution in the Infrared Amide I Spectral Region of β-Sheet Structures
Brauner, J. W., Dugan, C., & Mendelsohn, R. (2000) · Journal of the American Chemical Society · doi:10.1021/ja992522o · Cited by 140 · cited 2× · see citing works
“This can be used to separate the amide I bands of two proteins or a protein and a peptide for binding studies [369,370], to probe the local secondary structure of peptides [188,211,371 – 375] or to determine band shifts due to hydrogen bonding to water [194,195].”
BackgroundMethod
Gas phase infrared spectra of oxonium hydrate ions from 2 to 5 μ
Schwarz, H. A. (1977) · The Journal of Chemical Physics · doi:10.1063/1.434748 · Cited by 140 · cited 1× · see citing works
“In particular, the isolated (i.e. non-solvated) Eigen cation H 3 O + (H 2 O) 3 has a characteristic absorption at 2665 cm − 1 (OH stretch) [297,298] and the isolated Zundel cation H 2 O ⋯ H + ⋯ OH 2 near 1750 cm − 1 (HOH bend) and 1050 cm − 1 (O ⋯ H + ⋯ O stretch or bend) [297,299].”
Background
Amide I modes in the N-methylacetamide dimer and glycine dipeptide analog: Diagonal force constants
Ham, S., & Cho, M. (2003) · The Journal of Chemical Physics · doi:10.1063/1.1559681 · Cited by 139 · cited 1× · see citing works
“These quantities are calculated at two [199] or four [113,198 – 200] atoms of the amide group, at six atoms of NMA [197,200], or at up to 65 sites of the amide group [201] and related to the amide I frequency via ab initio quantum chemical calculations.”
Background
Evidence for the protonation of two internal carboxylic groups during the photocycle of bacteriorhodopsin
Siebert, F., Mäntele, W., & Kreutz, W. (1982) · FEBS Letters · doi:10.1016/0014-5793(82)80021-5 · Cited by 137 · cited 1× · see citing works
“Of particular importance was the identification of the proton transporting groups from the early detection of protonated carboxyl groups [376,378] to the assignment to specific residues or a localised protonated water cluster using isotopic labeling [384 – 386] and site-directed mutagenesis…”
Beziehungen zwischen Bindungsl�ngen und Bindungsst�rken in Oxidstrukturen
Allmann, R. (1975) · Monatshefte für Chemie - Chemical Monthly · doi:10.1007/bf00902183 · Cited by 137 · cited 1× · see citing works
“As bond strength and bond length are directly related [59,84 – 86], bond distortions smaller than 1 pm in the course of a catalytic reaction can be monitored with astonishing accuracy.”
Background
[20] Infrared spectroscopy applied to biochemical and biological problems
Siebert, F. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)46022-5 · Cited by 136 · cited 4× · see citing works
“This makes infrared spectroscopy a valuable tool for the investigation of protein structure [1 – 11] of the molecular mechanism of protein reactions [2,10 – 35] and Further advantages of infrared spectroscopy are a large application range from small soluble proteins to large membrane proteins, a…”
BackgroundMethodInfluential
Protein Secondary Structure from Fourier Transform Infrared and/or Circular Dichroism Spectra
Pribic, R., Vanstokkum, I. H. M., Chapman, D., Haris, P. I., & Bloemendal, M. (1993) · Analytical Biochemistry · doi:10.1006/abio.1993.1511 · Cited by 136 · see citing works
Effects of hydration on the structure, vibrational wavenumbers, vibrational force field and resonance raman intensities ofN-methylacetamide
Torii, H., Tatsumi, T., & Tasumi, M. (1998) · Journal of Raman Spectroscopy · doi:10.1002/(sici)1097-4555(199806)29:6 · Cited by 136 · see citing works
Predictions of Secondary Structure using Statistical Analyses of Electronic and Vibrational Circular Dichroism and Fourier Transform Infrared Spectra of Proteins in H2O
Baumruk, V., Pančoška, P., & Keiderling, T. A. (1996) · Journal of Molecular Biology · doi:10.1006/jmbi.1996.0357 · Cited by 136 · cited 1× · see citing works
“…the amide I band with component bands [10,220,228] after identifying their position with band narrowing techniques [229 – 232] and (ii) decomposing the amide I band into basis spectra which have been calculated from a calibration set of spectra from proteins with known structure [10,233 – 238].”
Method
A New Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy Method for the Study of Proteins in Solution
Oberg, K. A., & Fink, A. L. (1998) · Analytical Biochemistry · doi:10.1006/abio.1997.2486 · Cited by 136 · cited 2× · see citing works
“For protein samples, usually a protein film is prepared on the crystal surface [121,125,127,128], often simply by drying, and a buffer is placed on top of the film.”
BackgroundInfluential
Application of FTIR Spectroscopy to the Structural Study on the Function of Bacteriorhodopsin
Maeda, A. (1995) · Israel Journal of Chemistry · doi:10.1002/ijch.199500038 · Cited by 135 · cited 1× · see citing works
“These experiments provide spatially resolved information about functionally important water molecules, for example in bacteriorhodopsin [16,282 – 287], rhodopsin [16,283,288], sensory rhodopsin [289], photo-system II [290] and cytochrome c oxidase [291].”
Background
The importance of cooperativity for the properties of liquid water
Luck, W. A. P. (1998) · Journal of Molecular Structure · doi:10.1016/s0022-2860(98)00343-3 · Cited by 134 · cited 2× · see citing works
“Infrared spectroscopy of liquid water [274 – 276] and water clusters [277] has been reviewed recently.”
Background
Structure of a Histidine Ligand in the Photosynthetic Oxygen-Evolving Complex As Studied by Light-Induced Fourier Transform Infrared Difference Spectroscopy
Noguchi, T., Inoue, Y., & Tang, X.-S. (1999) · Biochemistry · doi:10.1021/bi990631+ · Cited by 133 · cited 3× · see citing works
“…groups [79], Arg, Asn [152,154,155,424], Asp [152,154,155,432,433], Cys [434], Gln [152,154,155,435], Glu [154,155,432,433], His − [65,426], HisH [65,154,426], HisH 2+ [64,65,155], Lys [152,154,427], Phe [154], Pro [429,436,437], Ser [79,434,438,439], Thr [79,438], Trp, [162,430,440,441], Tyr…”
Background
Fourier transform infrared study of proteins with parallel β-chains
Susi, H., & Byler, D. M. (1987) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(87)90367-5 · Cited by 132 · see citing works
Amide I modes of tripeptides: Hessian matrix reconstruction and isotope effects
Ham, S., Cha, S., Choi, J., & Cho, M. (2003) · The Journal of Chemical Physics · doi:10.1063/1.1581855 · Cited by 132 · cited 1× · see citing works
“These have been outlined and tested against quantum chemical calculations of peptides [187,208,209].”
Method
Light-flash physiology with synthetic photosensitive compounds.
Gurney, A. M., & Lester, H. A. (1987) · Physiological Reviews · doi:10.1152/physrev.1987.67.2.583 · Cited by 132 · cited 1× · see citing works
“These molecules are termed caged compounds and have been used for 30 years to study biological reactions [311 – 317].”
Background
INFRARED SPECTRUM OF THE H3O+ ION IN AQUEOUS SOLUTIONS
Falk, M., & Giguère, P. A. (1957) · Canadian Journal of Chemistry · doi:10.1139/v57-160 · Cited by 131 · cited 1× · see citing works
“An acidic aqueous solution exhibits a broad continuous absorption between 1000 and 3100 cm − 1 and additional bands with respect to neutral water near 1200, 1740, and 2900 cm − 1 [269,300 – 303] consistent with the presence of both, the Eigen and the Zundel forms of the hydrated proton [303].”
Background
Do Parallel β-Helix Proteins Have a Unique Fourier Transform Infrared Spectrum?
Khurana, R., & Fink, A. L. (2000) · Biophysical Journal · doi:10.1016/s0006-3495(00)76657-4 · Cited by 128 · cited 3× · see citing works
“However, as discussed above, similar spectra are expected for finite or twisted β -sheets [175,176,203,212] and there is no experimental evidence for a difference between the frequencies of parallel and antiparallel β -sheet [218,220].”
Background
Infrared spectroelectrochemistry of bacteriochlorophylls and bacteriopheophytins: Implications for the binding of the pigments in the reaction center from photosynthetic bacteria
Mäntele, W., Wollenweber, A. M., Nabedryk, E., & Breton, J. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.22.8468 · Cited by 127 · cited 1× · see citing works
“This is illustrated well by model studies on isolated biological cofactors involved in photosynthesis [80 – 83] that allowed the assignment of signals in the protein spectra to specific molecular groups of the cofactors and in consequence statements about their protein environment [12,13, 21,22].”
Method
FT‐IR and Raman vibrational microspectroscopies used for spectral biodiagnosis of human tissues
Lin, S., Li, M., & Cheng, W. (2007) · Journal of Spectroscopy · doi:10.1155/2007/278765 · Cited by 127 · see citing works
Reaction-Induced Infrared Difference Spectroscopy for the Study of Protein Reaction Mechanisms
Zscherp, C., & Barth, A. (2001) · Biochemistry · doi:10.1021/bi002567y · Cited by 125 · cited 2× · see citing works
“More information on this method can be found in reviews [12,21,30,32].”
BackgroundMethodSelf-citation
Nanosecond Time-Resolved Infrared Spectroscopy with a Dispersive Scanning Spectrometer
Yuzawa, T., Kato, C., George, M. W., & Hamaguchi, H. (1994) · Applied Spectroscopy · doi:10.1366/000370294774368947 · Cited by 123 · see citing works
Two-Dimensional Fourier Transform Near-Infrared Spectroscopy Study of Heat Denaturation of Ovalbumin in Aqueous Solutions
Wang, Y., Murayama, K., Myojo, Y., Tsenkova, R. N., Hayashi, N., & Ozaki, Y. (1998) · The Journal of Physical Chemistry B · doi:10.1021/jp9816115 · Cited by 122 · cited 1× · see citing works
“An alternative assignment of the amide B band to the stretching vibration of intramolecularly hydrogen bonded NH groups has recently found experimental support [164].”
Background
Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy
Souvignier, G., & Gerwert, K. B. (1992) · Biophysical Journal · doi:10.1016/s0006-3495(92)81722-8 · Cited by 121 · cited 1× · see citing works
“…made it possible to apply time-resolved techniques like single wavelength measurements with a global source [377 – 379], stroboscopic FTIR spectroscopy [380,381] and the step scan technique [144,382,383] which require numerous repetitions of the flash-induced experiment on a single sample.”
Background
Raman Markers of Nonaromatic Side Chains in an α-Helix Assembly: Ala, Asp, Glu, Gly, Ile, Leu, Lys, Ser, and Val Residues of Phage fd Subunits,
Overman, S. A., & Thomas, G. J. (1999) · Biochemistry · doi:10.1021/bi982901e · Cited by 121 · see citing works
Lifetimes of intermediates in the β-sheet to α-helix transition of β-lactoglobulin by using a diffusional IR mixer
Kauffmann, E., Darnton, N. C., Austin, R. H., Batt, C. A., & Gerwert, K. B. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.101122898 · Cited by 119 · cited 5× · see citing works
“Recently, a number of flow cells have been developed that enable mixing experiments [36,117 – 119].”
BackgroundMethodInfluential
H+ and OH− ions in aqueous solutions vibrational spectra of hydrates
Librovich, N. B., Sakun, V. P., & Sokolov, N. D. (1979) · Chemical Physics · doi:10.1016/0301-0104(79)80155-x · Cited by 119 · see citing works
Evidence for a tyrosine protonation change during the primary phototransition of bacteriorhodopsin at low temperature.
Rothschild, K. J., Roepe, P. D., Ahl, P. L., Earnest, T. N., Bogomolni, R. A., Gupta, S. K. D., Mulliken, C. M., & Herzfeld, J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.2.347 · Cited by 118 · cited 1× · see citing works
“…Glu [154,155,432,433], His − [65,426], HisH [65,154,426], HisH 2+ [64,65,155], Lys [152,154,427], Phe [154], Pro [429,436,437], Ser [79,434,438,439], Thr [79,438], Trp, [162,430,440,441], Tyr [64,66,67,152,154,155,442,443]. those in a spectral window free of overlap by bands from other groups.”
Background
Structure, stability, and receptor interaction of cholera toxin as studied by Fourier-transform infrared spectroscopy
Surewicz, W. K., Leddy, J. J., & Mantsch, H. H. (1990) · Biochemistry · doi:10.1021/bi00487a017 · Cited by 118 · see citing works
Residue Specific Resolution of Protein Folding Dynamics Using Isotope-Edited Infrared Temperature Jump Spectroscopy
Brewer, S. H., Song, B., Raleigh, D. P., & Dyer, R. B. (2007) · Biochemistry · doi:10.1021/bi602372y · Cited by 118 · see citing works
Physiological and Pharmacological Manipulations with Light Flashes
Lester, H. A., & Nerbonne, J. M. (1982) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.11.060182.001055 · Cited by 118 · see citing works
Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy.
Forge, V., Troullier, A., Reinstädler, D., Dupont, Y., & Naumann, D. (2000) · Nature Structural Biology · doi:10.1038/71286 · Cited by 117 · cited 1× · see citing works
“This approach has been used in studies of the Ca 2+ -ATPase pump mechanism [349] of the photoactive yellow protein photocycle [350], and of protein folding studies [36,38,42,43].”
Method
High resolution infrared spectra of water vapor
Fraley, P. E., & Rao, K. N. (1969) · Journal of Molecular Spectroscopy · doi:10.1016/0022-2852(69)90112-x · Cited by 117 · see citing works
Time-Resolved Infrared Spectroscopy of Intermediates and Products from Photolysis of 1-(2-Nitrophenyl)ethyl Phosphates: Reaction of the 2-Nitrosoacetophenone Byproduct with Thiols
Barth, A., Corrie, J. E. T., Gradwell, M. J., Maeda, Y., Mäntele, W., Meier, T., & Trentham, D. R. (1997) · Journal of the American Chemical Society · doi:10.1021/ja964430u · Cited by 115 · see citing works
Self-citation
Infrared Amide I‘ Band of the Coiled Coil
Reisdorf, W. C., & Krimm, S. (1996) · Biochemistry · doi:10.1021/bi951589v · Cited by 115 · cited 2× · see citing works
“For α -helices there is also evidence for an effect of hydrogen bonding on the vibrational frequency since solvated helices (i.e. helices forming hydrogen bonds also to solvent molecules) absorb approximately 20 cm − 1 lower than non-solvated helices [40,192 – 195].”
Background
Fourier transform methods for spectral resolution enhancement
Mantsch, H. H., Moffatt, D. J., & Casal, H. L. (1988) · Journal of Molecular Structure · doi:10.1016/0022-2860(88)80061-9 · Cited by 114 · see citing works
Isotope-Edited Infrared Spectroscopy of Helical Peptides
Decatur, S. M., & Antonic, J. (1999) · Journal of the American Chemical Society · doi:10.1021/ja991279q · Cited by 113 · see citing works
Protein secondary structure from FT-IR spectroscopy: correlation with dihedral angles from three-dimensional Ramachandran plots
Jackson, M., & Mantsch, H. H. (1991) · Canadian Journal of Chemistry · doi:10.1139/v91-240 · Cited by 113 · cited 1× · see citing works
“In addition to these effects, which are discussed below, changing the dielectric constant of the environment from 1 to 80 (water) reduces the calculated frequency for NMA by 30 cm − 1 [171] as suggested earlier for protein amide groups [172].”
Background
Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy
Belasco, J. G., & Knowles, J. R. (1980) · Biochemistry · doi:10.1021/bi00544a012 · Cited by 112 · cited 2× · see citing works
“…and proteins are investigated, as illustrated by studies on the binding of CO [264] and O 2 [357] to hemoglobin, of O 2 [357] to myoglobin, of carbonyl groups to triosephosphate isomerase [266] and phospholipase A 2 [358], and of phosphate groups to Ras [91,114,359,360] and Ca 2+ -ATPase [361].”
BackgroundMethod
Carboxyl group protonation upon reduction of the Paracoccus denitrificans cytochrome c oxidase: direct evidence by FTIR spectroscopy
Hellwig, P., Rost, B., Kaiser, U., Ostermeier, C., Michel, H., & Mäntele, W. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00342-0 · Cited by 112 · cited 1× · see citing works
“Cytochrome c oxidases and related heme-copper oxidases have been studied with a variety of infrared spectroscopic techniques as reviewed previously [32] including photodissociation of carbon monoxide (CO) [402], electrochemistry [334], photoreduction [345] and ATR spectroscopy [403,404].”
Background
Nonresonance Raman Difference Spectroscopy: A General Probe of Protein Structure, Ligand Binding, Enzymatic Catalysis, and the Structures of Other Biomacromolecules
Callender, R. H., & Deng, H. (1994) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.bb.23.060194.001243 · Cited by 112 · cited 1× · see citing works
“In Raman studies [54], favourable binding enthalpies with respect to water as large as − 60 kJ/mol have been detected for C _ O groups of substrates bound to enzymes.”
Background
Intensities and other spectral parameters of infrared amide bands of polypeptides in the α‐helical form
Chirgadze, Y. N., & Бражников, Е. В. (1974) · Biopolymers · doi:10.1002/bip.1974.360130902 · Cited by 111 · cited 1× · see citing works
“The band position of the main band shifts down with increasing helix length [174], when the helix is bent in coiled coils [192,213] and when the helix is solvent exposed (absorption maximum at 1640 – 1650 cm − 1 in H 2 O, at 1629 – 1640 cm − 1 in 2 H 2 O) [180,214 – 216].”
Background
D38 Is an Essential Part of the Proton Translocation Pathway in Bacteriorhodopsin
Riesle, J., Oesterhelt, D., Dencher, N. A., & Heberle, J. (1996) · Biochemistry · doi:10.1021/bi9600456 · Cited by 110 · cited 1× · see citing works
“Infrared spectroscopy has detected protonated water clusters in proteins, for example in a bacterial reaction centre [302] and in bacteriorhodopsin [304 – 307], where the localisation of the proton is affected by mutation of nearby amino acids [307].”
Background
Methods to study protein folding by stopped-flow FT-IR
Fabian, H. (2004) · Methods · doi:10.1016/j.ymeth.2004.03.004 · Cited by 109 · cited 1× · see citing works
“Nevertheless, successful applications of mixing devices have been reported, as reviewed recently [244], first with the larger pathlength of 50 μ m for 2 H 2 O [118] and subsequently with 20 μ m [117] and around 10 μ m for 1 H 2 O [36,119].”
Background
Conformational geometry and vibrational frequencies of nucleic acid chains
Brown, E. B., & Peticolas, W. L. (1975) · Biopolymers · doi:10.1002/bip.1975.360140614 · Cited by 109 · cited 1× · see citing works
“Hydrogen bonding to PO 2 − groups lowers the observed band position of the symmetric stretching vibration by 3 to 20 cm − 1 and of the antisymmetric stretching vibration by 20 – 34 cm − 1 [104 – 107] with a single hydrogen bond contributing 16 cm − 1 in a nitrogen matrix [107].”
Background
Fourier Transform Infrared Difference Spectroscopy of Photosystem II Tyrosine D Using Site-Directed Mutagenesis and Specific Isotope Labeling
Hienerwadel, R., Boussac, A., Breton, J., Diner, B. A., & Berthomieu, C. (1997) · Biochemistry · doi:10.1021/bi971521a · Cited by 108 · cited 2× · see citing works
“…Glu [154,155,432,433], His − [65,426], HisH [65,154,426], HisH 2+ [64,65,155], Lys [152,154,427], Phe [154], Pro [429,436,437], Ser [79,434,438,439], Thr [79,438], Trp, [162,430,440,441], Tyr [64,66,67,152,154,155,442,443]. those in a spectral window free of overlap by bands from other groups.”
Background
FTIR Spectroscopy of Alanine-Based Peptides: Assignment of the Amide I′ Modes for Random Coil and Helix
Martinez, G. V., & Millhauser, G. L. (1995) · Journal of Structural Biology · doi:10.1006/jsbi.1995.1002 · Cited by 107 · see citing works
Infrared studies of interaction between metal ions and Ca2+‐binding proteins Marker bands for identifying the types of coordination of the side‐chain COO− groups to metal ions in pike parvalbumin (pI = 4.10)
Nara, M., Tasumi, M., Tanokura, M., Hiraoki, T., Yazawa, M., & Tsutsumi, A. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00645-8 · Cited by 106 · cited 2× · see citing works
“…the carboxylate absorption sensitive to the mode of cation chelation [95 – 97] and has been used in studies of several Ca 2+ binding proteins [98,99]; (ii) the sensitivity of P \ O or V \ O stretching vibrations of phosphates or vanadates on the bond angle [100], applied to myosin [89] and Ras…”
BackgroundMethod

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Obtaining information about protein secondary structures in aqueous solution using Fourier transform IR spectroscopy
Yang, H., Yang, S., Kong, J., Dong, A., & Yu, S. (2015) · Nature Protocols · doi:10.1038/nprot.2015.024 · Cited by 1,293 · see citing works
Raman and infrared spectroscopy of carbohydrates: A review
Wiercigroch, E., Szafraniec, E., Czamara, K., Pacia, M. Z., Majzner, K., Kochan, K., Kaczor, A., Barańśka, M., & Małek, K. (2017) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2017.05.045 · Cited by 1,078 · see citing works
Fourier transform infrared (FTIR) spectroscopy
Berthomieu, C., & Hienerwadel, R. (2009) · Photosynthesis Research · doi:10.1007/s11120-009-9439-x · Cited by 798 · see citing works
“Amino acid side chains have a number of characteristic normal modes in the mid infrared (Venyaminov and Kalnin 1990a; Barth 2007).”
Background
Surface-Enhanced Infrared Spectroscopy Using Resonant Nanoantennas
Neubrech, F., Huck, C., Weber, K., Pucci, A., & Giessen, H. W. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00743 · Cited by 642 · see citing works
FTIR analysis of natural and synthetic collagen
Riaz, T., Zeeshan, R., Zarif, F., Ilyas, K., Muhammad, N., Safi, S. Z., Rahim, A., Rizvi, S. A. A., & Rehman, I. U. (2018) · Applied Spectroscopy Reviews · doi:10.1080/05704928.2018.1426595 · Cited by 628 · see citing works
“1253 cm¡1, His’ v(CN) and d(CH) at 1104, 1090, 1106, and 1094 cm¡1, Thr’s n(CO) at 1075–1150 cm¡1 (NC) at 1092 cm¡1, Ser’s v(CO) or v(CC) at 983 cm¡1, v(NC), d(CH), and v(CC) at 1064 cm¡1, gt CH2 at 1063–1295 cm¡1, v(CC) and d (CH) at 1012–1016 cm¡1 (157).”
Computing vibrational spectra from ab initio molecular dynamics
Thomas, M. A., Brehm, M., Fligg, R., Vöhringer, P., & Kirchner, B. (2013) · Physical Chemistry Chemical Physics · doi:10.1039/c3cp44302g · Cited by 593 · see citing works
Enhanced Activity of Enzymes Encapsulated in Hydrophilic Metal–Organic Frameworks
Liang, W., Xu, H., Carraro, F., Maddigan, N. K., Li, Q., Bell, S. G., Huang, D. M., Tarzia, A., Solomon, M. B., Amenitsch, H. W., et al. (2019) · Journal of the American Chemical Society · doi:10.1021/jacs.8b10302 · Cited by 560 · see citing works
Angle-multiplexed all-dielectric metasurfaces for broadband molecular fingerprint retrieval
Leitis, A., Tittl, A., Liu, M., Lee, B. H., Gu, M. B., Kivshar, Y. S., & Altug, H. (2019) · Science Advances · doi:10.1126/sciadv.aaw2871 · Cited by 546 · see citing works
“Chemically specific optical detection is enabled by the distinct absorption signatures of chemical and biological analytes at infrared (IR) frequencies (9, 10).”
Background
Secondary structure of food proteins by Fourier transform spectroscopy in the mid-infrared region
Carbonaro, M., & Nucara, A. (2009) · Amino Acids · doi:10.1007/s00726-009-0274-3 · Cited by 530 · see citing works
“Nine normal modes are generated for the amide band of proteins and peptides ( Barth 2007 ).”
BackgroundMethodInfluential
Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: a Fourier transform infrared (FT-IR) spectroscopic study
Carbonaro, M., Maselli, P., & Nucara, A. (2011) · Amino Acids · doi:10.1007/s00726-011-1151-4 · Cited by 466 · see citing works
A New Artificial Urine Protocol to Better Imitate Human Urine
Sarıgül, N., Korkmaz, F., & Kurultak, İ. (2019) · Scientific Reports · doi:10.1038/s41598-019-56693-4 · Cited by 462 · see citing works
ATR-FTIR: A “rejuvenated” tool to investigate amyloid proteins
Sarroukh, R., Goormaghtigh, E., Ruysschaert, J., & Raussens, V. (2013) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2013.04.012 · Cited by 449 · see citing works
“vibrations (for a complete description of this method sees the following references [103,104]).”
Physicochemical Stability of Monoclonal Antibodies: A Review
Basle, Y. L., Chennell, P., Tokhadzé, N., Astier, A., & Sautou, V. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.08.009 · Cited by 437 · see citing works
Vibrational Spectroscopic Map, Vibrational Spectroscopy, and Intermolecular Interaction
Baiz, C. R., Błasiak, B., Bredenbeck, J., Cho, M., Choi, J., Corcelli, S. A., Dijkstra, A. G., Feng, C.-J., Garrett-Roe, S., Ge, N., et al. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00813 · Cited by 420 · see citing works
In-situ ultra-sensitive infrared absorption spectroscopy of biomolecule interactions in real time with plasmonic nanoantennas
Adato, R., & Altug, H. (2013) · Nature Communications · doi:10.1038/ncomms3154 · Cited by 406 · see citing works
Formation of Fluorescent Metal (Au, Ag) Nanoclusters Capped in Bovine Serum Albumin Followed by Fluorescence and Spectroscopy
Guével, X. L., Hötzer, B., Jung, G., Hollemeyer, K., Trouillet, V., & Schneider, M. (2011) · The Journal of Physical Chemistry C · doi:10.1021/jp111820b · Cited by 384 · see citing works
Self-assembly of extracellular vesicle-like metal–organic framework nanoparticles for protection and intracellular delivery of biofunctional proteins
Cheng, G., Li, W., Ha, L., Han, X., Hao, S., Wan, Y., Wang, Z., Dong, F., Zou, X., Mao, Y., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b03584 · Cited by 371 · see citing works
Effect of ultrasound treatments on functional properties and structure of millet protein concentrate
Nazari, B., Mohammadifar, M. A., Shojaee‐Aliabadi, S., Feizollahi, E., & Mirmoghtadaie, L. (2017) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2017.10.002 · Cited by 353 · see citing works
“These increase in wave number according to the fact that frequency of stretching vibration reduced because of hydrogen bond formation [41].”
Background
Relationship between Secondary Structure and Surface Hydrophobicity of Soybean Protein Isolate Subjected to Heat Treatment
Wang, Z., Li, Y., Jiang, L., Qi, B., & Zhou, L. (2014) · Journal of Chemistry · doi:10.1155/2014/475389 · Cited by 343 · see citing works
“The amide I mode originates mainly from the C=O stretching vibration of the polypeptide backbone [32].”
Background
Pulse proteins: secondary structure, functionality and applications
Shevkani, K., Singh, N., Chen, Y., Kaur, A., & Yu, L. F. (2019) · Journal of Food Science and Technology · doi:10.1007/s13197-019-03723-8 · Cited by 342 · see citing works
“Table 1 represents the assignments of amide I band of FT-IR spectra to the secondary structure components of different plant proteins (Susi and Byler 1988; Kavanagh et al. 2000; Ellepola et al. 2005; Barth 2007; Carbonaro et al. 2012).”
Background
Supramolecular-Enhanced Charge Transfer within Entangled Polyamide Chains as the Origin of the Universal Blue Fluorescence of Polymer Carbon Dots
Vallan, L., Urriolabeitia, E. P., Ruipérez, F., Matxain, J. M., Cantón-Vitoria, R., Tagmatarchis, N., Benito, A. M., & Maser, W. K. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b06051 · Cited by 341 · see citing works
Infrared Difference Spectroscopy of Proteins: From Bands to Bonds
Lorenz, V. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00449 · Cited by 336 · see citing works
Infrared and Raman chemical imaging and spectroscopy at the nanoscale
Kurouski, D., Dazzi, A., Zenobi, R., & Centrone, A. (2020) · Chemical Society Reviews · doi:10.1039/c8cs00916c · Cited by 324 · see citing works
Non-dispersive infrared multi-gas sensing via nanoantenna integrated narrowband detectors
Tan, X., Zhang, H., Li, J., Wan, H., Guo, Q., Zhu, H., Liu, H., & Yi, F. (2020) · Nature Communications · doi:10.1038/s41467-020-19085-1 · Cited by 317 · see citing works
Interactions between gelatin and sodium alginate: UV and FTIR studies
Derkach, S. R., Voron’ko, N. G., Sokolan, N. I., Kolotova, D. S., & Kuchina, Y. A. (2019) · Journal of Dispersion Science and Technology · doi:10.1080/01932691.2019.1611437 · Cited by 311 · see citing works
“The Amide I band is the most sensitive to changes in the secondary structure of the protein.([28,44]) The Amide I band was resolved into six component peaks which are clearly seen on the second derivative spectra (Figure 3b).”
BackgroundMethod
A Biodegradable Antibacterial Nanocomposite Based on Oxidized Bacterial Nanocellulose for Rapid Hemostasis and Wound Healing
Yuan, H., Chen, L., & Hong, F. F. (2019) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.9b17732 · Cited by 307 · see citing works
Infrared spectroscopy and microscopy in cancer research and diagnosis.
Bellisola, G., & Sorio, C. (2012) · Europe PMC (PubMed Central) · Cited by 302 · see citing works
Potential of Raman spectroscopic techniques to study proteins
Kuhar, N., Sil, S., & Umapathy, S. (2021) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2021.119712 · Cited by 295 · see citing works
Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation
Ruggeri, F. S., Longo, G., Faggiano, S., Lipiec, E. W., Pastore, A., & Dietler, G. (2015) · Nature Communications · doi:10.1038/ncomms8831 · Cited by 289 · see citing works
Protein stability: a crystallographer's perspective
Deller, M. C., Kong, L., & Rupp, B. (2016) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x15024619 · Cited by 277 · see citing works
“Infrared spectroscopy can also be used to identify secondary-structure content (Barth, 2007).”
Effects of salt and sugar addition on the physicochemical properties and nanostructure of fish gelatin
Sow, L. C., & Yang, H. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.10.021 · Cited by 268 · see citing works
“Amide II also indicates the changes in the secondary structure of gelatin (Barth, 2007); however, this band is usually considered more sensitive to hydration than structural changes of protein (Benjakul, Oungbho, Visessanguan, Thiansilakul, & Roytrakul, 2009).”
BackgroundResultInfluential
Watching Proteins Wiggle: Mapping Structures with Two-Dimensional Infrared Spectroscopy
Ghosh, A., Ostrander, J. S., & Zanni, M. T. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00582 · Cited by 265 · see citing works
Investigating natural rubber composition with Fourier Transform Infrared (FT-IR) spectroscopy: A rapid and non-destructive method to determine both protein and lipid contents simultaneously
Rolère, S., Liengprayoon, S., Vaysse, L., Sainte‐Beuve, J., & Bonfils, F. (2015) · Polymer Testing · doi:10.1016/j.polymertesting.2015.02.011 · Cited by 262 · see citing works
Ultrasound driven conformational and physicochemical changes of soy protein hydrolysates
Tian, R., Feng, J., Huang, G., Tian, B., Zhang, Y., Jiang, L., & Sui, X. (2020) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2020.105202 · Cited by 260 · see citing works
Synergistic Solvation and Interface Regulations of Eco‐Friendly Silk Peptide Additive Enabling Stable Aqueous Zinc‐Ion Batteries
Wang, B., Zheng, R., Yang, W., Han, X. H., Hou, C., Zhang, Q., Li, Y., Li, K., & Wang, H. (2022) · Advanced Functional Materials · doi:10.1002/adfm.202112693 · Cited by 258 · see citing works
Biomolecular and bioanalytical applications of infrared spectroscopy – A review
Beć, K. B., Grabska, J., & Huck, C. W. (2020) · Analytica Chimica Acta · doi:10.1016/j.aca.2020.04.015 · Cited by 258 · see citing works
Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions
Usoltsev, D., Ситникова, В. Е., Kajava, A. V., & Uspenskaya, M. V. (2019) · Biomolecules · doi:10.3390/biom9080359 · Cited by 254 · see citing works
“Not only the hydrated films or solid-state can be easily studied, but also the aqueous solution [12], organic solvents, detergents, micelles, and phospholipid membranes, all these states allow to study the native structure of the protein [13], as well as to assess the effect of the medium on the protein structure.”
Background
Charge‐Induced Secondary Structure Transformation of Amyloid‐Derived Dipeptide Assemblies from β‐Sheet to α‐Helix
Xing, R., Yuan, C., Li, S., Song, J., Li, J., & Yan, X. (2017) · Angewandte Chemie International Edition · doi:10.1002/anie.201710642 · Cited by 250 · see citing works
Progress in infrared spectroscopy as an efficient tool for predicting protein secondary structure
Yang, S., Zhang, Q., Yang, H., Shi, H., Dong, A., Wang, L., & Yu, S. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.02.104 · Cited by 248 · see citing works
Comparative study on chemical compositions and properties of protein isolates from mung bean, black bean and bambara groundnut
Kudre, T. G., Benjakul, S., & Kishimura, H. (2013) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.6052 · Cited by 247 · see citing works
Intriguing role of water in protein-ligand binding studied by neutron crystallography on trypsin complexes
Schiebel, J., Gaspari, R., Wulsdorf, T., Ngo, K., Sohn, C., Schrader, T. E., Cavalli, A., Ostermann, A., Heine, A., & Klebe, G. (2018) · Nature Communications · doi:10.1038/s41467-018-05769-2 · Cited by 246 · see citing works
Mass Spectrometry-Based Protein Footprinting for Higher-Order Structure Analysis: Fundamentals and Applications
Liu, X. R., Zhang, M. M., & Gross, M. L. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00815 · Cited by 241 · see citing works
Protein Characteristics that Affect the Quality of Vital Wheat Gluten to be Used in Baking: A Review
Ortolan, F., & Steel, C. J. (2017) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12259 · Cited by 243 · see citing works
Protein adsorption onto nanomaterials for the development of biosensors and analytical devices: A review
Bhakta, S. A., Evans, E. J., Benavidez, T. E., & García, C. D. (2014) · Analytica Chimica Acta · doi:10.1016/j.aca.2014.10.031 · Cited by 242 · see citing works
“Other techniques [91] used to support research related to protein adsorption include capillary electrophoresis [99], mass spectrometry [100, 101] and particle mass spectrometry [102] (to identify and quantify proteins through fragmentation), various vibrational spectroscopictechniques [103, 104] (to study protein/subs…”
Method
An infrared spectroscopy approach to follow β-sheet formation in peptide amyloid assemblies
Seo, J., Hoffmann, W., Warnke, S., Huang, X., Gewinner, S., Schöllkopf, W., Bowers, M. T., von Helden, G., & Pagel, K. (2016) · Nature Chemistry · doi:10.1038/nchem.2615 · Cited by 238 · see citing works
Fourier transform infrared spectroscopic technique for analysis of inorganic materials: a review
Al-Amin, K., Kawsar, M., Mamun, M. A.-A., & Hossain, M. S. (2025) · Nanoscale Advances · doi:10.1039/d5na00522a · Cited by 233 · see citing works
Particles in Therapeutic Protein Formulations, Part 1: Overview of Analytical Methods
Zölls, S., Tantipolphan, R., Wiggenhorn, M., Winter, G., Jiskoot, W., Frieß, W., & Hawe, A. (2011) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.23001 · Cited by 231 · see citing works
Facile Synthesis of Enhanced Fluorescent Gold–Silver Bimetallic Nanocluster and Its Application for Highly Sensitive Detection of Inorganic Pyrophosphatase Activity
Zhou, Q., Lin, Y., Xu, M., Gao, Z., Yang, H., & Tang, D. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.6b02543 · Cited by 231 · see citing works
Physicochemical properties and antioxidant activities of tree peony (Paeonia suffruticosa Andr.) seed protein hydrolysates obtained with different proteases
Wang, Y., Wang, C., Wang, S., Li, Y., Mo, H., & He, J. (2020) · Food Chemistry · doi:10.1016/j.foodchem.2020.128765 · Cited by 230 · see citing works
C‐Type Cytochromes Wire Electricity‐Producing Bacteria to Electrodes
Busalmen, J. P., Esteve‐Núñez, A., Berná, A., & Feliu, J. M. (2008) · Angewandte Chemie International Edition · doi:10.1002/anie.200801310 · Cited by 224 · see citing works
Secondary structures of synthetic polypeptide polymers
Bonduelle, C. V. (2017) · Polymer Chemistry · doi:10.1039/c7py01725a · Cited by 222 · see citing works
Fourier Transform Infrared (FTIR) Spectroscopy to Analyse Human Blood over the Last 20 Years: A Review towards Lab-on-a-Chip Devices
Fadlelmoula, A., Pinho, D., Carvalho, V. H., Catarino, S. O., & Minas, G. M. H. (2022) · Micromachines · doi:10.3390/mi13020187 · Cited by 220 · see citing works
“The bands of amides I and II are usually used to analyse the secondary protein structure [27].”
Method
Protein–Phenolic Interactions as a Factor Affecting the Physicochemical Properties of White Bean Proteins
Sęczyk, Ł., Świeca, M., Kapusta, I. T., & Gawlik‐Dziki, U. (2019) · Molecules · doi:10.3390/molecules24030408 · Cited by 216 · see citing works
“Barth reported that amide I and amide II vibration modes strongly depend on the secondary structure of proteins, and they are hardly affected by the nature of their side chains; thus, they are suitable for analysis of secondary structure; however, the correlation between structure and frequency is more straightforward…”
Background
The role of protein characteristics in the formation and fluorescence of Au nanoclusters
Xu, Y., Sherwood, J. A., Qin, Y., Crowley, D., Bonizzoni, M., & Bao, Y. (2013) · Nanoscale · doi:10.1039/c3nr06040c · Cited by 215 · see citing works
Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods
Pignataro, M. F., Herrera, M. G., & Dodero, V. I. (2020) · Molecules · doi:10.3390/molecules25204854 · Cited by 215 · see citing works
Cold gelation of curcumin loaded whey protein aggregates mixed with k-carrageenan: Impact of gel microstructure on the gastrointestinal fate of curcumin
Alavi, F., Emam-djomeh, Z., Yarmand, M., Salami, M., Momen, S., & Moosavi-Movahedi, A. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.07.012 · Cited by 192 · see citing works
Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation
Ghosh, D., Singh, P. K., Sahay, S., Jha, N. N., Jacob, R. S., Sen, S., Kumar, A., Riek, R., & Maji, S. K. (2015) · Scientific Reports · doi:10.1038/srep09228 · Cited by 213 · see citing works
Characterization of extracellular vesicles by IR spectroscopy: Fast and simple classification based on amide and C H stretching vibrations
Mihály, J., Deák, R., Szigyártó, I. C., Bóta, A., Beke‐Somfai, T., & Varga, Z. (2016) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2016.12.005 · Cited by 212 · see citing works
Soybean straw nanocellulose produced by enzymatic or acid treatment as a reinforcing filler in soy protein isolate films
Martelli‐Tosi, M., Masson, M. M., da Silva, N. C., Esposto, B. S., Barros, T. T., ASSIS, O. B. G., & Tapia‐Blácido, D. R. (2018) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2018.06.053 · Cited by 212 · see citing works
Characterization of fibrillated antioxidant whey protein hydrolysate and comparison with fibrillated protein solution
Mohammadian, M., & Madadlou, A. (2015) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2015.06.022 · Cited by 211 · see citing works
Structure and Dynamics of Interfacial Peptides and Proteins from Vibrational Sum-Frequency Generation Spectroscopy
Hosseinpour, S., Roeters, S. J., Bonn, M., Peukert, W., Woutersen, S., & Weidner, T. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00410 · Cited by 211 · see citing works
Molecular pathology via IR and Raman spectral imaging
Diem, M., Mazur, A. I., Lenau, K., Schubert, J., Bird, B., Miljković, M., Krafft, C., & Popp, J. (2013) · Journal of Biophotonics · doi:10.1002/jbio.201300131 · Cited by 209 · see citing works
Effect of low moisture extrusion on a pea protein isolate’s expansion, solubility, molecular weight distribution and secondary structure as determined by Fourier Transform Infrared Spectroscopy (FTIR)
Beck, S. M., Knoerzer, K., & Arcot, J. (2017) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2017.06.037 · Cited by 209 · see citing works
Composite pullulan-whey protein nanofibers made by electrospinning: Impact of process parameters on fiber morphology and physical properties
Drosou, C., Krokida, M. K., & Βiliaderis, C. G. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.11.014 · Cited by 209 · see citing works
FTIR and Raman spectroscopic studies of selenium nanoparticles synthesised by the bacterium Azospirillum thiophilum
Tugarova, A. V., Mamchenkova, P. V., Dyatlova, Y. A., & Kamnev, A. A. (2017) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2017.11.050 · Cited by 209 · see citing works
Electric field stimulates production of highly conductive microbial OmcZ nanowires
Yalcin, S. E., O’Brien, J. P., Gu, Y., Reiss, K. M., Yi, S. M., Jain, R., Srikanth, V., Dahl, P. J., Huynh, W., Vu, D., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0623-9 · Cited by 205 · see citing works
Changes in molecular structure of extracellular polymeric substances (EPS) with temperature in relation to sludge macro-physical properties
Peng, S., Hu, A., Ai, J., Zhang, W., & Wang, D. (2021) · Water Research · doi:10.1016/j.watres.2021.117316 · Cited by 205 · see citing works
Mussel adhesion is dictated by time-regulated secretion and molecular conformation of mussel adhesive proteins
Petrone, L., Kumar, A., Sutanto, C. N., Patil, N. J., Kannan, S., Palaniappan, A., Amini, S., Zappone, B., Verma, C. S., & Miserez, A. (2015) · Nature Communications · doi:10.1038/ncomms9737 · Cited by 203 · see citing works
Self healing hydrogels composed of amyloid nano fibrils for cell culture and stem cell differentiation
Jacob, R. S., Ghosh, D., Singh, P. K., Basu, S. K., Jha, N. N., Das, S., Sukul, P. K., Patil, S. P., Sathaye, S., Kumar, A., et al. (2015) · Biomaterials · doi:10.1016/j.biomaterials.2015.03.002 · Cited by 203 · see citing works
“After establishing the amyloidogenic nature of the gel network, we used FTIR spectroscopy to check whether the peptides in gel state were composed of b-sheet-rich structure [70].”
Method
Biomaterials from Ultrasonication-Induced Silk Fibroin−Hyaluronic Acid Hydrogels
Hu, X., Lü, Q., Sun, L., Cebe, P., Wang, X., Zhang, X., & Kaplan, D. L. (2010) · Biomacromolecules · doi:10.1021/bm1010504 · Cited by 201 · see citing works
Non-conventional fluorescent biogenic and synthetic polymers without aromatic rings
Ye, R., Liu, Y., Zhang, H., Su, H., Zhang, Y., Xu, L., Hu, R., Kwok, R. T. K., Wong, K. S., Lam, J. W. Y., et al. (2017) · Polymer Chemistry · doi:10.1039/c7py00154a · Cited by 200 · see citing works
Amino acids as co-amorphous stabilizers for poorly water-soluble drugs – Part 2: Molecular interactions
Löbmann, K., Laitinen, R., Strachan, C. J., Rades, T., & Grohganz, H. (2013) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2013.03.026 · Cited by 195 · see citing works
“Minor changes were also observed for the amide I and II vibrations of both amino acids in the region between 1555 and 1659 cm 1 [10,14].”
BackgroundResultInfluential
Sunflower protein films incorporated with clove essential oil have potential application for the preservation of fish patties
Salgado, P. R., López-Caballero, M. E., Gómez-Guillén, M. C., Mauri, A. N., & Montero, P. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.02.008 · Cited by 196 · see citing works
The antibacterial activity of Magainin I immobilized onto mixed thiols Self-Assembled Monolayers
Humblot, V., Yala, J.-F., Thébault, P., Boukerma, K., Héquet, A., Berjeaud, J., & Pradier, C. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2009.03.025 · Cited by 193 · see citing works
Interpolymeric complexing between egg white proteins and xanthan gum: Effect of salt and protein/polysaccharide ratio
Souza, C. J. F., & Garcia‐Rojas, E. E. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.11.032 · Cited by 192 · see citing works
Ultrastrong and Bioactive Nanostructured Bio-Based Composites
Mittal, N., Jansson, R., Widhe, M., Benselfelt, T., Håkansson, K. M. O., Lundell, F., Hedhammar, M., & Söderberg, D. (2017) · ACS Nano · doi:10.1021/acsnano.7b02305 · Cited by 192 · see citing works
Synthesis and characterization of human transferrin-stabilized gold nanoclusters
Guével, X. L., Schneider‐Daum, N., & Schneider, M. (2011) · Nanotechnology · doi:10.1088/0957-4484/22/27/275103 · Cited by 191 · see citing works
Valorisation of chicken feathers: Characterisation of chemical properties
Tesfaye, T., Sithole, B. B., Ramjugernath, D., & Chunilall, V. (2017) · Waste Management · doi:10.1016/j.wasman.2017.06.050 · Cited by 190 · see citing works
Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate
Gong, K., Shi, A.-M., Liu, H., Liu, L., Hu, H., Adhikari, B., & Wang, Q. (2015) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2015.09.011 · Cited by 188 · see citing works
Authentication and Quality Assessment of Meat Products by Fourier-Transform Infrared (FTIR) Spectroscopy
Candoğan, K., Altuntaş, E. G., & İğci, N. (2020) · Food Engineering Reviews · doi:10.1007/s12393-020-09251-y · Cited by 187 · see citing works
Protein-directed, hydrogen-bonded biohybrid framework
Chen, G., Huang, S., Shen, Y., Kou, X., Ma, X., Huang, S., Tong, Q., Ma, K., Chen, W. L., Wang, P., et al. (2021) · Chem · doi:10.1016/j.chempr.2021.07.003 · Cited by 184 · see citing works
Trehalose Renders the Dauer Larva of Caenorhabditis elegans Resistant to Extreme Desiccation
Erkut, C., Penkov, S., Khesbak, H., Vorkel, D., Verbavatz, J., Fahmy, K., & Kurzchalia, T. V. (2011) · Current Biology · doi:10.1016/j.cub.2011.06.064 · Cited by 183 · see citing works
Evaluation of electrospun poly (vinyl alcohol)-based nanofiber mats incorporated with Zataria multiflora essential oil as potential wound dressing
Torabiardekani, N., Khorram, M., Zomorodian, K., Yazdanpanah, S., Veisi, H., & Veisi, H. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.12.085 · Cited by 181 · see citing works
Review: Detection and quantification of proteins in human urine
Aitekenov, S., Gaipov, A., & Bukasov, R. (2020) · Talanta · doi:10.1016/j.talanta.2020.121718 · Cited by 181 · see citing works
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“Even thought, around this wavenumber region (1370e1230 cm 1) previous works reported the contribution of proteins (Band amide III) (Barth & Zscherp, 2002), phenolic esters attached to polysaccharides (S en e, McCann, Wilson, & Grinter, 1994), and methyl ester groups (CH3), which could come, for instance, from 4-O-Megl…”
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“Hence a wealth of information on proteins may be derived from their IR spectrum, as detailed in [6].”
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“The center frequencies of the amide I (1636 cm) and amide II bands (1549 cm) indicate a b-sheet structure for the protein, agreeing with previous studies (8, 54).”
BackgroundResult
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“FTIR as a quantitative tool was used with KBr pellet and potassium ferricyanide, K3Fe(CN)6 (2117 cm (1)), as an internal standard, to get characteristic parameters of chemical groups in the samples (Barth, 2007; Joshi, Kalyanasundaram, & Balasubramanian, 2013).”
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Authors: Barth, A.
Affiliations: Stockholm University (SE)
Corresponding author: Barth, Andreas
ORCID: Barth, Andreas
Venue: Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher: Elsevier BV
Published: 2007-09
Volume: 1767
Issue: 9
Pages: 1073-1101
ISSN: 0005-2728 (ISSN-L)
DOI: 10.1016/j.bbabio.2007.06.004
OpenAlex: W1992045220
Cited by: 5,129
References: 444
Citations by year: 2026: 521 · 2025: 475 · 2024: 403 · 2023: 406 · 2022: 407 · 2021: 427 · 2020: 465 · 2019: 357 · 2018: 311 · 2017: 313 · 2016: 237 · 2015: 187 · 2014: 148 · 2013: 132 · 2012: 97
FWCI: 3.85
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 2147 d)
Locations: Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Spectroscopy Techniques in Biomedical and Chemical Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Physical Sciences › Physics and Astronomy › Atomic and Molecular Physics, and Optics › Spectroscopy and Quantum Chemical Studies
Keywords: infrared spectroscopy, proteins, mid-infrared spectra, protein reactions, protein structure
MeSH terms: Amides, Amino Acids, Enzymes, Hydrogen Bonding, Hydrogen-Ion Concentration, Models, Chemical, Molecular Conformation, Oscillometry, Oxidation-Reduction, Proteins, Protons, Spectrophotometry, Infrared, Time Factors, Water, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared

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