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PMID: 8019132 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.

Journal of biomolecular NMR ·Vol. 4 ·No. 2 ·1994-03-00 ·Pages 171-80

Wishart DS, Sykes BD

Abstract

A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements.

MeSH Terms
Amino Acids/analysis Carbon Isotopes Interferon-gamma/chemistry Magnetic Resonance Spectroscopy/methods Protein Structure, Secondary Solvents
Chemicals
Amino Acids Carbon Isotopes Solvents Interferon-gamma
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wishart D S
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Sykes B D
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Article Info
Journal
Journal of biomolecular NMR
Abbr.
J Biomol NMR
ISSN
0925-2738
DOI
10.1007/BF00175245
Published
1994-03-00
Pages
171-80
Language
English
Region
Netherlands
NLM ID
9110829
Subset
IM
External Links
PubMed source DOI: 10.1007/BF00175245 View journal details
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