Incremental contribution to protein stability from a β hairpin "finger":: Limits on the stability of designed β hairpin peptides

被引：12

作者：

Searle, MS ^{[1
]}

Platt, GW ^{[1
]}

Bofill, R ^{[1
]}

Simpson, SA ^{[1
]}

Ciani, B ^{[1
]}

机构：

[1] Univ Nottingham, Sch Chem, Ctr Biomol Sci, Nottingham NG7 2RD, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2004年 / 43卷 / 15期

关键词：

NMR spectroscopy; protein folding; protein modifications; proteins; structure elucidation;

D O I：

10.1002/anie.200352955

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Back to the fold: A new method to determining the stability of a β hairpin is described. A β hairpin forming sequence (β4) is introduced into native ubiquitin (see structure) enabling the contribution to protein stability of this structural motif to be estimated. This data provides both an upper limit on stability for autonomously folding β hairpins, and a spectroscopic reference state for estimating the stability of related peptides in solution.

引用

页码：1991 / 1994

页数：4

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