Structural Consequences of Accommodation of Four Non-cognate Amino Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin

Volume: 333, Issue: 4, Pages: 845 - 861
Published: Oct 1, 2003
Abstract
Crystal structures of P1 Gly, Val, Leu and Phe bovine pancreatic trypsin inhibitor (BPTI) variants in complex with two serine proteinases, bovine trypsin and chymotrypsin, have been determined. The association constants for the four mutants with the two enzymes show that the enlargement of the volume of the P1 residue is accompanied by an increase of the binding energy, which is more pronounced for bovine chymotrypsin. Since the conformation of...
Paper Details
Title
Structural Consequences of Accommodation of Four Non-cognate Amino Acid Residues in the S1 Pocket of Bovine Trypsin and Chymotrypsin
Published Date
Oct 1, 2003
Volume
333
Issue
4
Pages
845 - 861
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