Capturing intrinsic nanomechanics of allostery

被引：0
|
作者：
Marszalek, Piotr E. [1 ]
机构：
[1] Duke Univ, Dept Mech Engn & Mat Sci, Durham, NC 27708 USA
来源：
BIOPHYSICAL JOURNAL | 2022年 / 121卷 / 23期
关键词：
SUBSTRATE-BINDING DOMAIN;
D O I：
10.1016/j.bpj.2022.10.037
中图分类号：
Q6 [生物物理学];
学科分类号：
071011 ;
摘要：
The Hsp70 chaperone exploits allosteric communication between its substrate binding domain and its nucleotide binding domain to regulate the loading and release of misfolded polypeptides in an ATP-hydrolysis-dependent manner. In this issue of Biophysical Journal, Singh, Rief, and Zoldak report an exquisitely detailed study of the nanomechanical aspects of the allosteric mechanism in DnaK, an Escherichia coli heat shock protein 70 chaperone.
引用
收藏
页码：4415 / 4416
页数：2
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