变构调节
变构酶
计算生物学
计算机科学
生物物理学
化学
生物
生物化学
酶
作者
Hesam N. Motlagh,James O. Wrabl,Jing Li,Vincent J. Hilser
出处
期刊:Nature
[Springer Nature]
日期:2014-04-15
卷期号:508 (7496): 331-339
被引量:1227
摘要
Allostery is the process by which biological macromolecules (mostly proteins) transmit the effect of binding at one site to another, often distal, functional site, allowing for regulation of activity. Recent experimental observations demonstrating that allostery can be facilitated by dynamic and intrinsically disordered proteins have resulted in a new paradigm for understanding allosteric mechanisms, which focuses on the conformational ensemble and the statistical nature of the interactions responsible for the transmission of information. Analysis of allosteric ensembles reveals a rich spectrum of regulatory strategies, as well as a framework to unify the description of allosteric mechanisms from different systems.
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