Coupling of global and local vibrational modes in dynamic allostery of proteins
Coupling of global and local vibrational modes in dynamic allostery of proteins
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DOI：
10.1529/biophysj.106.082180
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发表时间：
2006-09-01
影响因子：
3.4
通讯作者：
McLeish, Tom C. B.
中科院分区：
文献类型：
--
作者：
Hawkins, Rhoda J.;McLeish, Tom C. B.
现在人们认识到，蛋白质内部的全局动力学在许多蛋白质的变构功能中起着重要作用。蛋白质的变化。效应器结合的灵活性会影响远距离结合的熵成本。我们提出了一个粗粒度的模型，用于描述由于快的局域模式与慢的整体模式的耦合而导致的这种熵变构的潜在放大。我们展示了这种耦合是如何产生大的补偿性熵和热项的。该模型与Met阻滞剂实验中的量热和核磁共振数据相对应。
It is now recognized that internal global protein dynamics play an important role in the allosteric function of many proteins. Alterations of protein. exibility on effector binding affect the entropic cost of binding at a distant site. We present a coarse-grained model for a potential amplification of such entropic allostery due to coupling of fast, localized modes to the slow, global modes. We show how such coupling can give rise to large compensating entropic and enthalpic terms. The model corresponds to the pattern of calorimetry and NMR data from experiments on the Met repressor.