The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Estimation of amino acid residue side‐chain absorption in the infrared spectra of protein solutions in heavy water
Abstract
The values of maximum frequencies, intensities, and other spectral parameters of the main absorption bands of amino acid residue side‐chain groups have been obtained in the 1500–1800‐cm−1 region for solutions in heavy water at pD 1–12. It is shown that absorption of residues of asparagine, glutamine, aspartic and glutamic acids, arginine, and tyrosine must be taken into account in quantitative studies of the infrared spectra of polypeptide and protein solutions in heavy water. Examples of separating out the amide I band for ribonuclease A in heavy water are given.
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Citations
Cites
Structure and stability of biological macromolecules
Timasheff, S. N., & Fasman, G. D. (1969) · Cited by 1,316
The Sequence of Amino Acid Residues in Bovine Pancreatic Ribonuclease: Revisions and Confirmations
Smyth, D. G., Stein, W. H., & Moore, S. (1963) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83984-4 · Cited by 563
Chirgadze, Y. N., Shestopalov, B. V., & Venyaminov, S. Y. (1973) · Biopolymers · doi:10.1002/bip.1973.360120610 · Cited by 159
Self-citationChirgadze, Y. N., & Бражников, Е. В. (1974) · Biopolymers · doi:10.1002/bip.1974.360130902 · Cited by 111
Self-citationSome characteristic frequencies of amino acids
Tsuboi, M., Takenishi, T., & Nakamuba, A. (1963) · Spectrochimica Acta · doi:10.1016/0371-1951(63)80105-8 · Cited by 56
Fraser, R., & Suzuki, E. (1970) · Elsevier eBooks · doi:10.1016/b978-0-12-440102-0.50010-3 · Cited by 10
Cited by
Infrared spectroscopy of proteins
Barth, A. (2007) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2007.06.004 · Cited by 5,129
“…vibration References: aliphatic groups [79], Arg, Asn [152,154,155,424], Asp [152,154,155,432,433], Cys [434], Gln [152,154,155,435], Glu [154,155,432,433], His − [65,426], HisH [65,154,426], HisH 2+ [64,65,155], Lys [152,154,427], Phe [154], Pro [429,436,437], Ser [79,434,438,439], Thr…”
BackgroundInfluentialGoormaghtigh, E., Ruysschaert, J.-M., & Raussens, V. (2006) · Biophysical Journal · doi:10.1529/biophysj.105.072017 · Cited by 417
Infrared Difference Spectroscopy of Proteins: From Bands to Bonds
Lorenz-Fonfria, V. A. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00449 · Cited by 325
Metadata
- Authors
- Chirgadze, Y. N., Fedorov, O. V., & Trushina, N. P.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1975-04
- Volume
- 14
- Issue
- 4
- Pages
- 679-694
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W2134880328
- Cited by
- 478
- References
- 6
- FWCI
- 2.15
- Type
- journal article
- Language
- en
- Open access
- closed
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- Chirgadze, Y. N., Fedorov, O. V., & Trushina, N. P. (1975). Estimation of amino acid residue side‐chain absorption in the infrared spectra of protein solutions in heavy water. Biopolymers. https://doi.org/10.1002/bip.1975.360140402
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