An effective strategy for the design of proteins with enhanced mechanical stability

被引：23

作者：

Borgia, Alessandro ^{[1
]}

Steward, Annette ^{[1
]}

Clarke, Jane ^{[1
]}

机构：

[1] Univ Cambridge, Chem Lab, MRC, Ctr Prot Engn, Cambridge CB2 1EW, England

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2008年 / 47卷 / 36期

基金：

英国惠康基金; 英国医学研究理事会;

关键词：

force microscopy; mechanical properties; protein engineering; titin;

D O I：

10.1002/anie.200801761

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

(Graph Presented) Titinic strength: The mechanical resistance of titin domain I27 (see picture, left) was increased by substituting residues from a stronger homologue in regions of the protein important for mechanical strength (red). The unfolding profile of I27st (see picture, right) shows that the mechanical strength is significantly increased compared to wild-type I27 (black arrow). © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：6900 / 6903

页数：4

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