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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Fast protein folding kinetics
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Fast protein folding kinetics

机译：快速蛋白质折叠动力学

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摘要

Proteins are complex molecules, yet their folding kinetics is often fast (microseconds) and simple, involving only a single exponential function of time (called two-state kinetics). The main model for two-state kinetics has been transition-state theory, where an energy barrier defines a slow step to reach an improbable structure. But how can barriers explain fast processes, such as folding? We study a simple model with rigorous kinetics that explains the high speed instead as a result of the microscopic parallelization of folding trajectories. The single exponential results from a separation of timescales; the parallelization of routes is high at the start of folding and low thereafter. The ensemble of rate-limiting chain conformations is different from in transition-state theory; it is broad, overlaps with the denatured state, is not aligned along a single reaction coordinate, and involves well populated, rather than improbable, structures.
机译：蛋白质是复杂的分子，但是它们的折叠动力学通常是快速的（微秒）和简单的，仅涉及时间的单一指数函数（称为二态动力学）。两态动力学的主要模型是过渡态理论，其中能垒定义了达到不可能结构的缓慢步骤。但是障碍如何解释快速的过程，例如折叠？我们研究了具有严格动力学的简单模型，该模型解释了高速运动，而不是折叠轨迹的微观平行化的结果。单一指数是由于时间尺度的分离而产生的；路线的平行度在折叠开始时较高，此后较低。限速链构象的集合不同于过渡态理论。它是宽泛的，与变性状态重叠，未沿着单个反应坐标对齐，并且涉及人口稠密而不是不可能的结构。

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