Mixed helices -: A general folding pattern in homologous peptides?

被引：72

作者：

Baldauf, C ^{[1
]}

Günther, R ^{[1
]}

Hofmann, HJ ^{[1
]}

机构：

[1] Univ Leipzig, Inst Biochem, D-04103 Leipzig, Germany

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2004年 / 43卷 / 12期

关键词：

ab initio calculations; conformational analysis; foldamers; peptides; secondary structure;

D O I：

10.1002/anie.200353249

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

You may now exchange rings! "Mixed helices" along a peptide sequence, in which rings of different sizes are held together by hydrogen bonds in alternating directions (see picture), prove to be a general folding principle in homologous α-, β-, γ-, and δ-peptides.

引用

页码：1594 / 1597

页数：4

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