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The nature of trypsin-pancreatic trypsin inhibitor binding: free energy calculation of Tyr39-->Phe39 mutation in trypsin

Melo, A.; Ramos, M.J.

Journal of Peptide Research: Official Journal of the American Peptide Society 50(5): 382-387

1997


ISSN/ISBN: 1397-002X
PMID: 9401923
DOI: 10.1111/j.1399-3011.1997.tb01198.x
Accession: 047686440

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 Tyr39-Ile19 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.

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