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Article

A fluorescence stopped-flow kinetic study of the conformational activation of alpha-chymotrypsin and several mutants.

Protein science : a publication of the Protein Society - 1 Sept 2004

Verheyden Gert, Matrai Janka, Volckaert Guido, Engelborghs Yves

Abstract excerpt

The kinetic activation parameters (activation free energy, activation free enthalpy, and activation free entropy change) of the conformational change of alpha-chymotrypsin from an inactive to the active conformation were determined after a pH jump from pH 11.0 to pH 6.8 by the fluorescence stopped-flow method. The conformational change was followed by measuring changes in the protein fluorescence. For the bovine...

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Identifiers

PMID: 15322291
DOI: 10.1110/ps.04709604
PMCID: PMC2280002

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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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