Article
Hydrolysis of small peptide substrates parallels binding of chymotrypsin inhibitor 2 for mutants of subtilisin BPN'.
FEBS letters - 13 Dec 1993
Eder J, Rheinnecker M, Fersht A R
Abstract excerpt
Variants of subtilisin BPN' that possess improved specificity towards isoleucine compared with alanine at the P4 position of small peptide substrates, were analysed for their ability to bind chymotrypsin inhibitor 2. The binding of the inhibitor with isoleucine (wild-type) and with alanine as the P4 residue parallels the hydrolysis of tetrapeptide substrates. There is a linear relationship between the free energy...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
