NMR structural analysis of a beta-hairpin peptide designed for DNA binding

被引：37

作者：

Maynard, AJ ^{[1
]}

Searle, MS ^{[1
]}

机构：

[1] UNIV NOTTINGHAM,DEPT CHEM,NOTTINGHAM NG7 2RD,ENGLAND

来源：

CHEMICAL COMMUNICATIONS | 1997年 / 14期

关键词：

D O I：

10.1039/a702593i

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

NMR and circular dichroism (CD) spectroscopy shows that an unconstrained 16 residue linear peptide folds autonomously in water into a beta-hairpin: the designed peptide adopts a conformation that mimics the anti-parallel beta-sheet DNA binding motif of the met repressor protein dimer with key residues for DNA recognition presented in the same positions and orientations principally on one face of the beta-hairpin template.

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收藏

页码：1297 / 1298

页数：2

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