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

• Tipo: Artigo em Revista Científica Internacional
• Data: 1997

Autores

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

Revista

Título: Journal of Peptide Research

Vol. 50

Páginas: 382-387

ISSN: 1397-002X

Editora: Blackwell

Indexação

ISI Web of Knowledge - 8 Citações

Scopus - 7 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 6