Prev. Article Next Article Table of Contents

Communication

Effects of H₂O and D₂O on Polyproline II Helical Structure

Brian W. Chellgren and Trevor P. Creamer*

Center for Structural Biology, Department of Molecular and Cellular Biochemistry, University of Kentucky, 800 Rose Street, Lexington, Kentucky 40536-0298

J. Am. Chem. Soc., 2004, 126 (45), pp 14734–14735

DOI: 10.1021/ja045425q

Publication Date (Web): October 26, 2004

In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

, Trevor.Creamer@uky.edu

Abstract

The interaction of solvent with a polypeptide chain is one of the primary factors controlling protein folding and stability. In biologically relevant systems, this solvent is most often water. Experimental estimates of the role of water in peptide folding can be obtained from solvent perturbation experiments. The simplest perturbant for H₂O water is its isotopic D₂O form. The solvation of peptides known to form P_II helices with D₂O versus H₂O increases their propensity to adopt the P_II conformation.

View: Full Text HTML | Hi-Res PDF