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Article

Probing weakly polar interactions in cytochrome c.

Protein science : a publication of the Protein Society - 1 Dec 1993

Auld D S, Young G B, Saunders A J, Doyle D F, Betz S F, Pielak G J

Abstract excerpt

Theoretical, statistical, and model studies suggest that proteins are stabilized by weakly polar attractions between sulfur atoms and properly oriented aromatic rings. The two sulfur-containing amino acids, methionine and cysteine, occur frequently among functional alleles in random mutant libraries of Saccharomyces cerevisiae iso-1-cytochrome c genes at positions that form a weakly polar aromatic-aromatic...

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Identifiers

PMID: 8298464
DOI: 10.1002/pro.5560021218
PMCID: PMC2142317

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