The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
The X‐Pro peptide bond as an nmr probe for conformational studies of flexible linear peptides
Abstract
The equilibrium between the cis and trans forms of X‐Pro peptide bonds can readily be measured in the 13 C nmr spectra. In the present paper we investigate how observation of this equilibrium could be used as an nmr probe for conformational studies of flexible polypeptide chains. The experiments include studies by 13 C nmr of a series of linear oligopeptides containing different X‐L‐Pro peptide bonds, with X = Gly, L‐Ala, L‐Leu, L‐Phe, D‐Ala, D‐Leu, and D‐Phe. Overall the study confirms that X‐Pro peptide bonds can generally be useful as 13 C nmr probes reporting the formation of nonrandom conformation in flexible polypeptide chains. It was found that the cis–trans equilibrium of X‐Pro is greatly affected by the side chain of X and the configuration of the α‐carbon atom of X. On the basis of these observations some general rules are suggested for a practical applications of the X‐Pro nmr probes in conformational studies of polypeptide chains.
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Citations
Cites
Conformation of Polypeptides and Proteins
Ramachandran, G. N., & Sasisekharan, V. (1968) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60402-7 · Cited by 2,938
The structure and action of proteins
Dickerson, R. E., & Geis, I. (1969) · Andalas University Repository (Andalas University) · Cited by 733
Chemistry and Biology of Peptides
Gitu, P. M., Hruby, V., Brown, W. S., & Muscio, F. (1972) · Cited by 614
Peptides, polypeptides and proteins
Malcolm, B. R. (1976) · Polymer · doi:10.1016/0032-3861(76)90166-x · Cited by 533
NMR in biological research: Peptides and proteins
Radda, G. K. (1977) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(77)90231-6 · Cited by 528
Carbon-13 magnetic resonance spectroscopy. Spectrum of proline in oligopeptides
Dorman, D. E., & Bovey, F. A. (1973) · The Journal of Organic Chemistry · doi:10.1021/jo00953a021 · Cited by 281
A novel approach for studies of the molecular conformations in flexible polypeptides
Wüthrich, K., & Grathwohl, C. (1974) · FEBS Letters · doi:10.1016/0014-5793(74)80674-5 · Cited by 69
Self-citation13C magnetic resonance study of the ionization of N-acetyl-dl-proline in aqueous solution
Bedford, G. R., & Sadler, P. J. (1974) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(74)90286-4 · Cited by 25
Proton Nuclear Magnetic Resonance Study of Corticotropins
Patel, D. J. (1971) · Macromolecules · doi:10.1021/ma60020a023 · Cited by 13
Cited by
Folding of immunogenic peptide fragments of proteins in water solution
Dyson, H. J., Rance, M., Houghten, R. A., Lerner, R. A., & Wright, P. E. (1988) · Journal of Molecular Biology · doi:10.1016/0022-2836(88)90446-9 · Cited by 733
Experimental studies of protein folding and unfolding
Creighton, T. E. (1979) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(79)90030-0 · Cited by 530
Folding of peptide fragments comprising the complete sequence of proteins
Dyson, H. J., Merutka, G., Waltho, J. P., Lerner, R. A., & Wright, P. E. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90633-u · Cited by 388
Side-chain effects on peptidyl-prolyl cis/trans isomerisation
Reimer, U., Scherer, G., Drewello, M., Kruber, S., Schutkowski, M., & Fischer, G. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1770 · Cited by 354
Aromatic–Proline Interactions: Electronically Tunable CH/π Interactions
Zondlo, N. J. (2013) · Accounts of Chemical Research · doi:10.1021/ar300087y · Cited by 318
Metadata
- Authors
- Grathwohl, C., & Wüthrich, K.
- Venue
- Biopolymers
- Publisher
- Wiley
- Published
- 1976-10
- Volume
- 15
- Issue
- 10
- Pages
- 2025-2041
- ISSN
- 0006-3525 (ISSN-L)
- 1097-0282
- OpenAlex
- W2089058369
- Cited by
- 272
- References
- 9
- FWCI
- 4.77
- Type
- journal article
- Language
- en
- Open access
- closed
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