Slaving: Solvent fluctuations dominate protein dynamics and functions
Slaving: Solvent fluctuations dominate protein dynamics and functions
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DOI：
10.1073/pnas.212637899
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发表时间：
2002-12-10
影响因子：
11.1
通讯作者：
Parak, FG
中科院分区：
文献类型：
--
作者：
Fenimore, PW;Frauenfelder, H;Parak, FG
蛋白质运动对机体功能至关重要。将蛋白质过程与周围溶剂的介电波动进行比较，可以发现它们分为两类：非奴役型和奴役型。非从工过程与溶剂运动无关；它们的速率由蛋白质的构象和振动动力学决定。从属过程与溶剂紧密耦合；它们的速率与溶剂波动速率具有近似相同的温度依赖性，但它们更小。由于温度依赖性是由活化焓决定的，我们提出溶剂负责活化焓，而蛋白质和水合壳层通过能量格局控制活化熵。键的形成是非奴隶过程的原型；通道的开启和关闭是典型的奴隶运动。奴隶运动的普遍存在突出了细胞和膜环境对蛋白质功能的重要性。
Protein motions are essential for function. Comparing protein processes with the dielectric fluctuations of the surrounding solvent shows that they fall into two classes: nonslaved and slaved. Nonslaved processes are independent of the solvent motions; their rates are determined by the protein conformation and vibrational dynamics. Slaved processes are tightly coupled to the solvent; their rates have approximately the same temperature dependence as the rate of the solvent fluctuations, but they are smaller. Because the temperature dependence is determined by the activation enthalpy, we propose that the solvent is responsible for the activation enthalpy, whereas the protein and the hydration shell control the activation entropy through the energy landscape. Bond formation is the prototype of nonslaved processes; opening and closing of channels are quintessential slaved motions. The prevalence of slaved motions highlights the importance of the environment in cells and membranes for the function of proteins.