Ontology highlight
ABSTRACT:
SUBMITTER: Haddad KC
PROVIDER: S-EPMC545854 | biostudies-other | 2005 Jan
REPOSITORIES: biostudies-other
Haddad Kristin Coffman KC Sudmeier James L JL Bachovchin Daniel A DA Bachovchin William W WW
Proceedings of the National Academy of Sciences of the United States of America 20050118 4
alpha-Lytic protease is a bacterial serine protease widely studied as a model system of enzyme catalysis. Here we report that lyophilization induces a structural change in the enzyme that is not reversed by redissolution in water. The structural change reduces the mobility of the active-site histidine residue and the catalytic activity of the enzyme. The application of mild pressure to solutions of the altered enzyme reverses the lyophilization-induced structural change and restores the mobility ...[more]