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

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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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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×
“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×
“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
Handbook of Vibrational Spectroscopy
(2006) · Wiley eBooks · doi:10.1002/0470027320 · Cited by 3,017
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×
“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
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×
“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 2,107
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 2,059 · cited 1×
“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
Handbook of vibrational spectroscopy
Chalmers, J. M., & Griffiths, P. R. (2002) · Cited by 1,838
Internal Reflection Spectroscopy
Harrick, N. J., & Hoffman, J. G. (1968) · Physics Today · doi:10.1063/1.3034675 · Cited by 1,725

Show all 444 references

Research works printed but not linked: 7

Palafox, 1998, Empirical correlations in vibrational spectroscopy, Trends Appl. Spectrosc., 2, 37
Mäntele, 1990, Application of tunable infrared diode lasers for the study of biochemical reactions: time-resolved vibrational spectroscopy of intermediates in the primary processes of photosynthesis, Spectrosc. Int., 2, 29
Torii, 1998, 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, J. Raman Spectrosc., 229, 81, 10.1002/(SICI)1097-4555(199801)29:1<81::AID-JRS214>3.0.CO;2-H · DOI
Corrie, 1993, Caged nucleotides and neurotransmitters, Vol. 2, 243
Williams, 1996, Fast events in protein folding: Helix melting and formation in a small peptide, Biochemistry, 35, 691, 10.1021/bi952217p · DOI
Cao, 1993, Proton transfer from Asp-96 to the bacteriorhodopsin Schiff base is caused by a decrease of the pKa of Asp-96 which follows a protein conformational change, Biochemistry, 32, 1981, 10.1021/bi00059a015 · DOI
Madec, 1978, Etude du spectre de vibration de la dl-serine et des ses dérivés deuteries, Can. J. Spectrosc., 23, 166

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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 207
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 200
“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
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
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
“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
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 205
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
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
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
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 198
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
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
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 185
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
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
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 189
Hydrogen-bonded organic framework biomimetic entrapment allowing non-native biocatalytic activity in enzyme
Chen, G., Tong, L., Huang, S., Huang, S., Zhu, F., & Ouyang, G. (2022) · Nature Communications · doi:10.1038/s41467-022-32454-2 · Cited by 183
“=O stretching and N-H bending 34 , respectively) were perturbed after encapsulation by HOF-101, further supporting the interfacial interaction between Cyt c and HOF-101 (Supplementary Fig.”
Modeling the IR Spectra of Aqueous Metal Carboxylate Complexes: Correlation between Bonding Geometry and Stretching Mode Wavenumber Shifts
Sutton, C. C. R., da Silva, G. F., & Franks, G. V. (2015) · Chemistry - A European Journal · doi:10.1002/chem.201406516 · Cited by 178
Advanced characterization of immobilized enzymes as heterogeneous biocatalysts
Bolivar, J. M., Eisl, I., & Nidetzky, B. (2015) · Catalysis Today · doi:10.1016/j.cattod.2015.05.004 · Cited by 178
Determination of the domain structure of the 7S and 11S globulins from soy proteins by XRD and FTIR
Chen, J., Chen, X., Zhu, Q., Chen, F., Zhao, X., & Ao, Q. (2012) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.5950 · Cited by 176
Peptide-Directed Assembly of Single-Helical Gold Nanoparticle Superstructures Exhibiting Intense Chiroptical Activity
Merg, A. D., Boatz, J. C., Mandal, A., Zhao, G., Mokashi‐Punekar, S., Liu, C., Wang, X., Zhang, P., van der Wel, P. C. A., & Rosi, N. L. (2016) · Journal of the American Chemical Society · doi:10.1021/jacs.6b07322 · Cited by 174
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Siddiqui, S., Ameen, F., Rehman, S. U., Sarwar, T., & Tabish, M. (2021) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2021.116200 · Cited by 173
Nanomaterials design and tests for neural tissue engineering
Saracino, G. A. A., Cigognini, D., Silva, D., Caprini, A., & Gelain, F. (2012) · Chemical Society Reviews · doi:10.1039/c2cs35065c · Cited by 172
Acacia senegal vs. Acacia seyal gums – Part 1: Composition and structure of hyperbranched plant exudates
Lopez-Torres, L., Nigen, M., Williams, P., Doco, T., & Sanchez, C. (2015) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2015.04.019 · Cited by 172
“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…”
Background
Mid-infrared spectroscopy for protein analysis: potential and challenges
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“Hence a wealth of information on proteins may be derived from their IR spectrum, as detailed in [6].”
Background
Nitrile groups as vibrational probes of biomolecular structure and dynamics: an overview
Lindquist, B. A., Furse, K. E., & Corcelli, S. A. (2009) · Physical Chemistry Chemical Physics · doi:10.1039/b908588b · Cited by 171
Interfacing Formate Dehydrogenase with Metal Oxides for the Reversible Electrocatalysis and Solar‐Driven Reduction of Carbon Dioxide
Miller, M., Robinson, W. E., Oliveira, A. R., Heidary, N., Kornienko, N., Warnan, J., Pereira, I. A. C., & Reisner, E. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201814419 · Cited by 169
Effects of high pressure processing on the thermal gelling properties of chicken breast myosin containing κ-carrageenan
Chen, X., Chen, C.-G., Zhou, Y.-Z., Li, P.-J., Ma, F., Nishiumi, T., & Suzuki, A. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.03.018 · Cited by 150
Infrared electric field sampled frequency comb spectroscopy
Kowligy, A. S., Timmers, H. R., Lind, A. J., Elu, U., Cruz, F. C., Schunemann, P. G., Biegert, J., & Diddams, S. A. (2019) · Science Advances · doi:10.1126/sciadv.aaw8794 · Cited by 166
“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
Bioactivity and nutritional properties of hardy kiwi fruit Actinidia arguta in comparison with Actinidia deliciosa ‘Hayward’ and Actinidia eriantha ‘Bidan’
Hanna Leontowicz, A., Maria Leontowicz, A., Latocha, P., Jesion, I., Park, Y., Katrich, E., Barasch, D., Nemirovski, A., & Gorinstein, S. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.08.127 · Cited by 163
“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).”
BackgroundMethod
Localizing normal modes in large molecules
Jacob, C. R., & Reiher, M. (2009) · The Journal of Chemical Physics · doi:10.1063/1.3077690 · Cited by 163
Toxicity assessment of metal oxide nano-pollutants on tomato (Solanum lycopersicon): A study on growth dynamics and plant cell death
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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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