ALPHA-HELIX FORMATION BY PEPTIDES OF DEFINED SEQUENCE

被引：112

作者：

BALDWIN, RL

机构：

[1] Department of Biochemistry, Stanford Medical Center, Stanford

来源：

BIOPHYSICAL CHEMISTRY | 1995年 / 55卷 / 1-2期

关键词：

HELIX-STABILIZING INTERACTION; HELIX PROPENSITY; N-CAP;

D O I：

10.1016/0301-4622(94)00146-B

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The factors controlling alpha-helix formation in water by peptides of defined sequence are beginning to be understood. The field is close to the point where the extent of helix formation can be predicted for peptides of any sequence. Our own approach to the problem, and the main results obtained by following this approach, are summarized below. The chief reason for studying alpha-helix formation by peptides is to understand precisely and in detail one part of the protein folding problem. Questions about peptide helix formation can be answered at a fundamental level, in terms of the physico-chemical mechanisms involved.

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页码：127 / 135

页数：9

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