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Article

Effects of tyrosine mutations on the conformational and oxidative folding of ribonuclease a: a comparative study.

Biochemistry - 12 May 2009

Gahl Robert F, Pradeep Lovy, Siegel Corey R, Xu Guoqiang, Scheraga Harold A

Abstract excerpt

Ribonuclease A (RNase A) undergoes more rapid conformational folding with its disulfide bonds intact than during oxidative folding from its reduced form. In this study, the effects of the mutants Y92G, Y92A, and Y92L on both the conformational and oxidative folding pathways were examined to determine the role of native interactions in different types of conformational searches for the biologically active...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 19344116
DOI: 10.1021/bi802362t
PMCID: PMC2677636

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Effects of tyrosine mutations on the conformational and oxidative folding of ribonuclease a: a comparative study.PMID 19344116Read ↗

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