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

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“Figure 3a also shows characteristic protein groups, namely, amide I (around 1640 cm−1), amide II (around 1527 cm−1), and amide III (around 1247 cm−1) (Barth 2007; Gulrajani et al. 2008).”
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“In fact, two of the characteristic bands of the polypeptide structure fall in this range, the amide I and the amide II [32].”
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“Protein modes also absorb in this region, and contributions of amide I and II bands may be expected around 1650 and 1550 cm (43).”
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“The peak at 658 cm−1, caused by the completely in-plane vibration of the O=C-N bond was shifted to 591 (P1-Zn), 570 (P2-Zn), and 597 cm−1 (P3-Zn) when peptide fractions were bound to zinc, which was caused by the increasing electron cloud density of O=CH2 and decreasing election cloud density of N-H, shifted [34,35].”
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“Notably, the amide I band is sensitive to the protein secondary structure [7,11].”
Background
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“In the absence of the stressing agent the second derivative spectrum is characterized by a band at ~1657 cm−1, mainly due to alpha-helix and random-coil structures of the whole cell proteins, and by a band at ~1639 cm−1, assigned to intramolecular native beta-sheets [19, 26], (Fig.”
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“FTIR spectra of neat firefly luciferase showed distinctive peaks at 1550 cm−1 and 1515 cm−1, which are amide-II vibrations characteristic of luciferase [20].”
Background
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“The amide II range (between 1,590 cm and 1,450 cm) involves coupled CN/NH vibrational modes of the protein backbone (31), as well as contributions from individual amino acids reorganizing or changing protonation states with the alkaline pH shift.”
BackgroundInfluential
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“In all conditions tested, the spectral profile of VF-1 is clearly different from the designed amyloid peptides [38,39] and transduction enhancing EF-C β-sheet nanofibrils [14], that exhibit typical and predominant features at 1695–1672cm−1 and 1638–1615cm−1 [40].”
Background
Assessment of growth phases of the diatom Ditylum brightwellii by FT-IR and Raman spectroscopy
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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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