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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Crossref · 10.1016/j.bbabio.2007.06.004

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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].”
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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×
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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
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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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“[26, 27] The”
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“These bands are conformationally sensitive to protein secondary structure and any bending, vibration, or stretching of the functional groups in these regions following processing is an indication of alteration in protein secondary structure (Barth, 2007).”
Background
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“6A) showed two spectral bands at 1624 and 1395 cm 1, corresponding to changes in the amide I absorption band of b-sheet proteins (Barth 2007; Kong and Yu 2007), and in the symmetric stretching of COO groups in amino acids and/or fatty acids (Legal et al. 1991; Belfer et al. 2005; Parikh and…”
BackgroundInfluential
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“To examine the secondary structure of the incubated PAAs, FTIR spectroscopy of these aggregates was performed (74).”
Method
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“2016; Barth 2007; Salunkhe et al.”

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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