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Article

Changing the transition state for protein (Un) folding.

Biochemistry - 11 Jun 1996

Doyle D F, Waldner J C, Parikh S, Alcazar-Roman L, Pielak G J

Abstract excerpt

(Un)folding transition states of Saccharomyces cerevisiae iso-1-ferri- and ferrocytochromes c were studied using equilibrium and kinetic denaturation experiments. The wild-type protein and the global suppressor variant, N52I (isoleucine replaces asparagine 52), were examined. Denaturation was induced by guanidinium chloride (GdmCI) and monitored by circular dichroism (CD) spectropolarimetry without stopped-flow...

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Source

Identifiers

PMID: 8652517
DOI: 10.1021/bi960409u

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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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