Probing protein-protein interactions by dynamic force correlation spectroscopy
Probing protein-protein interactions by dynamic force correlation spectroscopy
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DOI：
10.1103/physrevlett.95.168302
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发表时间：
2005-10-14
影响因子：
8.6
通讯作者：
Thirumalai, D
中科院分区：
文献类型：
--
作者：
Barsegov, V;Thirumalai, D
我们发展了一种单分子动态力光谱的形式来绘制蛋白质-蛋白质复合体(P1P2)的能量图景。在压缩-拉伸循环中可测量的非结合寿命的联合分布P(tau(1)，tau(2))说明了tau(1)的直方图不是泊松的，它解释了拉伸下蛋白质的内部松弛动力学。该理论被应用于蛋白质P-1从P1P2强制解离，蛋白质P-1被建模为蠕虫链。我们提出了一类新的实验，可以解决内部蛋白质动力学对解离寿命的影响。
We develop a formalism for single molecule dynamic force spectroscopy to map the energy landscape of protein-protein complex (P1P2). The joint distribution P(tau(1),tau(2)) of unbinding lifetimes tau(1) and tau(2), measurable in a compression-tension cycle, which accounts for the internal relaxation dynamics of the proteins under tension, shows that the histogram of tau(1) is not Poissonian. The theory is applied to the forced unbinding of protein P-1, modeled as a wormlike chain, from P1P2. We propose a new class of experiments which can resolve the effect of internal protein dynamics on the unbinding lifetimes.