Changing the transition state for protein (Un) folding.

doi:10.1021/bi960409u

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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 ind...

Topics

Asparagine
Calorimetry
Circular Dichroism
Cytochrome c Group
Cytochromes c
Genetic Variation
Guanidine
Guanidines
Isoleucine
Kinetics
Oxidation-Reduction
Protein Conformation
Protein Denaturation
Protein Folding
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sensitivity and Specificity
Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 8652517
DOI: 10.1021/bi960409u

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8652517-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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