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Article

A dynamic bundle of four adjacent hydrophobic segments in the denatured state of staphylococcal nuclease.

Protein science : a publication of the Protein Society - 1 Sept 1996

Wang Y, Shortle D

Abstract excerpt

In an earlier study of the denatured state of staphylococcal nuclease (Wang Y, Shortle D, 1995, Biochemistry 34:15895-15905), we reported evidence of a three-strand antiparallel beta sheet that persists at high urea concentrations and is stabilized by a local "non-native" interaction with four large hydrophobic residues. Because the amide proton resonances for all of the involved residues are severely broadened,...

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Identifiers

PMID: 8880914
DOI: 10.1002/pro.5560050916
PMCID: PMC2143551

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