The nature of trypsin-pancreatic trypsin inhibitor binding: Free energy calculation of Tys(39)->Phe(39) mutation in trypsin

• Type: Article in International Scientific Journal
• Date: 1997

Authors

Melo, A (Author) FCUP; Ramos, MJ (Author) FCUP

Journal

Title: Journal of Peptide Research

Vol. 50

Pages: 382-387

ISSN: 1397-002X

Publisher: Blackwell

Indexing

ISI Web of Knowledge - 8 Citations

Scopus - 7 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-001-ACR

Abstract (EN): The main goal of this work is the detailed study of the binding interactions in the trypsin-pancreatic trypsin inhibitor (PTI) complex and, here, we present how meaningful the Tyr(39)-Ile(19) interaction is to the stability of that particular complex using free energy methods. This knowledge should be very important in the design of new inhibitors for trypsin and enzymes homologous to it. In particular, it could help to decide whether it is possible to produce selective inhibitors for these enzymes by appropriate mutations of residues in the contact region of PTI. (C) Munksgaard 1997.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 6