Nonmechanical protein can have significant mechanical stability

被引：101

作者：

Cao, Y ^{[1
]}

Lam, C ^{[1
]}

Wang, MJ ^{[1
]}

Li, HB ^{[1
]}

机构：

[1] Univ British Columbia, Dept Chem, Vancouver, BC V6T 1Z1, Canada

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2006年 / 45卷 / 04期

关键词：

mechanical properties; protein unfolding; scanning probe microscopy; single-molecule studies;

D O I：

10.1002/anie.200502623

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The unique topology of the B1 immunoglobulin G (IgG) binding domain of streptococcal protein G (GB1) leads to its remarkable mechanical stability. This nonmechanical protein is shown to be mechanically stable and to unfold at about 180 pN (the force-extension curves (right) shown demonstrate the mechanical unraveling of each GB1 domain in the polyprotein which is made of direct tandem repeats of GB1 (left)). (Graph Presented). © 2006 Wiley-VCH Verlag GmbH & Co. KGaA.

引用

页码：642 / 645

页数：4

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