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Article

Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface.

Biochemistry - 14 Mar 1995

Pielak G J, Auld D S, Beasley J R, Betz S F, Cohen D S, Doyle D F, Finger S A, Fredericks Z L, Hilgen-Willis S, Saunders A J

Abstract excerpt

Random mutant libraries with substitutions at the interface between the N- and C-terminal helices of Saccharomyces cerevisiae iso-1-cytochrome c were screened. All residue combinations that have been identified in naturally occurring cytochrome c sequences are found in the libraries. Mutants with these combinations are biologically functional. Enthalpies, heat capacities, and midpoint temperatures of denaturation...

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Identifiers

PMID: 7880822
DOI: 10.1021/bi00010a017

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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