Reengineering a type II beta-turn as a potential helix nucleator .1. Crystal structure of Boc-Val-Pro-(D)Asp-Asp-Val-OMe monohydrate

Abstract

The crystal structure of Boc-Val(1)-Pro(2)-(D)Asp(3)-Asp(4)-Val(5)-OMe is described as a type II beta-turn reengineered into a potential helix nucleator. (D)Asp(3) in the peptide is responsible for the configurationally guided LD chiral type II beta-turn centered at Pro(2)-(D)Asp(3), as well as the partially developed LL chiral type I beta-turn centered at Asp(4)-Val(5) by acceptance of a conformation nucleating H-bond from Val(5)NH to its carboxylic oxygen. (C) Munksgaard 1997.