捕捉变构作用的固有纳米力学。
Capturing intrinsic nanomechanics of allostery.
机构信息
Department of Mechanical Engineering and Materials Science, Duke University, Durham, North Carolina.
出版信息
Biophys J. 2022 Dec 6;121(23):4415-4416. doi: 10.1016/j.bpj.2022.10.037. Epub 2022 Oct 29.
Abstract
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 Žoldák report an exquisitely detailed study of the nanomechanical aspects of the allosteric mechanism in DnaK, an Escherichia coli heat shock protein 70 chaperone.
摘要
Hsp70 伴侣蛋白利用其底物结合域和核苷酸结合域之间的变构通讯，以 ATP 水解依赖的方式调节错误折叠多肽的加载和释放。在本期《生物物理杂志》中，Singh、Rief 和Žoldák 报道了对大肠杆菌热休克蛋白 70 伴侣蛋白 DnaK 的变构机制的纳米力学方面的一项极其详细的研究。
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