The DOI matches its Crossref record; 440 of the 444 references it cites were found in a registry or an index.
Infrared spectroscopy of proteins
Open accessAbstract
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 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]
Citations
Cites
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].”
BackgroundInfluentialDeacon, 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…”
MethodHandbook 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…”
MethodVibrational 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].”
BackgroundInfluentialWhat vibrations tell about proteins
Barth, A., & Zscherp, C. (2002) · Quarterly Reviews of Biophysics · doi:10.1017/s0033583502003815 · Cited by 2,107
Self-citationThe 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 ].”
BackgroundAnoxygenic 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
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
Cited by
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Yang, H., Yang, S., Kong, J., Dong, A., & Yu, S. (2015) · Nature Protocols · doi:10.1038/nprot.2015.024 · Cited by 1,310
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
Fourier transform infrared (FTIR) spectroscopy
Berthomieu, C., & Hienerwadel, R. (2009) · Photosynthesis Research · doi:10.1007/s11120-009-9439-x · Cited by 798
“Amino acid side chains have a number of characteristic normal modes in the mid infrared (Venyaminov and Kalnin 1990a; Barth 2007).”
BackgroundSurface-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 651
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
“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).”
Metadata
- 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)
- 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
- 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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