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Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis

Evans, PA and Dobson, CM and Kautz, RA and Hatfull, G and Fox, RO (1987) Proline isomerism in staphylococcal nuclease characterized by NMR and site-directed mutagenesis. Nature, 329 (6136). 266 - 268. ISSN 0028-0836

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Abstract

Nuclear magnetic resonance (NMR) studies have shown that two distinct folded conformations of staphylococcal nuclease coexist in solution1 and that these two states can interconvert directly without passing through an unfolded state. These experiments have also revealed that the two forms have very different folding kinetics, although the possibility that one component is an obligatory intermediate for the folding of the other form could be discounted1. Here we report NMR data which show that alternative unfolded states are also distinguishable. These observations led us to hypothesize that cis/trans isomerism at a single peptide bond between a proline and its preceding residue might be the origin of the conformational multiplicity. Proline 117 was identified as a likely candidate for the site concerned and a mutant protein, in which Pro 117 was replaced by Gly, was constructed in order to test this. Alternative conformations are not observed in the spectrum of this mutant, lending powerful support to this hypothesis. © 1987 Nature Publishing Group.

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Details

Item Type: Article
Status: Published
Creators/Authors:
CreatorsEmailPitt UsernameORCID
Evans, PA
Dobson, CM
Kautz, RA
Hatfull, Ggfh@pitt.eduGFH
Fox, RO
Date: 1 January 1987
Date Type: Publication
Journal or Publication Title: Nature
Volume: 329
Number: 6136
Page Range: 266 - 268
DOI or Unique Handle: 10.1038/329266a0
Schools and Programs: Dietrich School of Arts and Sciences > Biological Sciences
Refereed: Yes
ISSN: 0028-0836
MeSH Headings: Isomerism; Magnetic Resonance Spectroscopy; Micrococcal Nuclease--genetics; Mutation; Proline; Protein Conformation
PubMed ID: 3627269
Date Deposited: 30 Jun 2015 14:30
Last Modified: 22 Jun 2021 12:56
URI: http://d-scholarship.pitt.edu/id/eprint/23507

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