Effects of H2O and D2O polyproline lane II helical structure

被引:47
作者
Chellgren, BW [1 ]
Creamer, TP [1 ]
机构
[1] Univ Kentucky, Dept Mol & Cellular Biochem, Ctr Struct Biol, Lexington, KY 40536 USA
关键词
D O I
10.1021/ja045425q
中图分类号
O6 [化学];
学科分类号
0703 [化学];
摘要
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 PII helices with D2O versus H2O increases their propensity to adopt the PII conformation. Copyright © 2004 American Chemical Society.
引用
收藏
页码:14734 / 14735
页数:2
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