肌红蛋白中蛋白质弛豫与配体结合及迁移的耦合。
Coupling of protein relaxation to ligand binding and migration in myoglobin.
作者信息
Agmon Noam
机构信息
Department of Physical Chemistry, The Hebrew University of Jerusalem, Jerusalem, Israel.
出版信息
Biophys J. 2004 Sep;87(3):1537-43. doi: 10.1529/biophysj.104.042929.
Abstract
Protein relaxation, ligand binding, and ligand migration into a hydrophobic cavity in myoglobin are unified by a bounded diffusion model which produces an accurate fit to complex ligand rebinding data over eight decades in time and a 160 K temperature range, in qualitative agreement with time-resolved x-ray crystallography. Protein relaxation operates in a cyclic manner to move the ligand away from the binding site.
摘要
蛋白质弛豫、配体结合以及配体向肌红蛋白疏水腔的迁移，由一个受限扩散模型统一起来。该模型能够在八个数量级的时间范围以及160K的温度范围内，对复杂的配体再结合数据进行精确拟合，这与时间分辨X射线晶体学在定性上是一致的。蛋白质弛豫以循环方式运作，将配体从结合位点移开。
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