Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances

Kurt Wüthrich, Martin Billeter, Werner Braun

Research output: Contribution to journalArticle

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Abstract

The use of proton-proton nuclear Overhauser enhancement (NOE) distance information for identification of polypeptide secondary structures in non-crystalline proteins was investigated by stereochemical studies of standard secondary structures and by statistical analyses of the secondary structures in the crystal conformations of a group of globular proteins. Both regular helix and β-sheet secondary structures were found to contain a dense network of short 1H-1H distances. The results obtained imply that the combined information on all these distances obtained from visual inspection of the two-dimensional NOE (NOESY) spectra is sufficient for determination of the helical and β-sheet secondary structures in small globular proteins. Furthermore, cis peptide bonds can be identified from unique, short sequential proton-proton distances. Limitations of this empirical approach are that the exact start or end of a helix may be difficult to define when the adjoining residues form a tight turn, and that unambiguous identification of tight turns can usually be obtained only in the hairpins of antiparallel β-structures. The short distances between protons in pentapeptide segments of the different secondary structures have been tabulated to provide a generally applicable guide for the analysis of NOESY spectra of proteins.

Original languageEnglish (US)
Pages (from-to)715-740
Number of pages26
JournalJournal of Molecular Biology
Volume180
Issue number3
DOIs
StatePublished - Dec 15 1984
Externally publishedYes

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Protons
Magnetic Resonance Spectroscopy
Observation
Peptides
Proteins
Spectrum Analysis

ASJC Scopus subject areas

  • Virology

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Polypeptide secondary structure determination by nuclear magnetic resonance observation of short proton-proton distances. / Wüthrich, Kurt; Billeter, Martin; Braun, Werner.

In: Journal of Molecular Biology, Vol. 180, No. 3, 15.12.1984, p. 715-740.

Research output: Contribution to journalArticle

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