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Infrared spectroscopy of proteins
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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]
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“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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“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…”
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“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…”
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“The amide II band is weak or absent in the Raman spectrum [151].”
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Self-citationThe Use and Misuse of FTIR Spectroscopy in the Determination of Protein Structure
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“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 ].”
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“{Kubelka, 2001 #4372}{Barth, 2007 #8162} This spectrum and all others contain a strong peak at 1673 cm -1 which is assigned to TFA counterions 46- 48 bound to NH3 + groups (in the R residue).”
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“Moreover, the amide I and amide II bands - mainly due to the C=O stretching and the NH bending of the peptide bond respectively - give information on the protein secondary structure [30], while the spectral range between 1000 and 800 cm-1 is very informative on nucleic acid absorption, since it is due in particular to…”
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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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