Ontology highlight
ABSTRACT:
SUBMITTER: Verheyden G
PROVIDER: S-EPMC2280002 | biostudies-literature | 2004 Sep
REPOSITORIES: biostudies-literature
Protein science : a publication of the Protein Society 20040901 9
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 wild-type protein, the same kinetic parameters are obtained as in the study of profl ...[more]