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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >How fast is protein hydrophobic collapse?
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How fast is protein hydrophobic collapse?

机译：蛋白质疏水性崩溃速度有多快？

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One of the most recurring questions in protein folding refers to the interplay between formation of secondary structure and hydrophobic collapse. In contrast with secondary structure, it is hard to isolate hydrophobic collapse from other folding events. We have directly measured the dynamics of protein hydrophobic collapse in the absence of competing processes. Collapse was triggered with laser-induced temperature jumps in the acid-denatured form of a simple protein and monitored by fluorescence resonance energy transfer between probes placed at the protein ends. The relaxation time for hydrophobic collapse is only approximately 60 ns at 305 K, even faster than secondary structure formation. At higher temperatures, as the protein becomes increasingly compact by a stronger hydrophobic force, we observe a slowdown of the dynamics of collapse. This dynamic hydrophobic effect is a high-temperature analogue of the dynamic glass transition predicted by theory. Our results indicate that in physiological conditions many proteins will initiate folding by collapsing to an unstructured globule. Local motions will presumably drive the following search for native structure in the collapsed globule.
机译：蛋白质折叠中最经常出现的问题之一是二级结构的形成与疏水性折叠之间的相互作用。与二级结构相反，很难将疏水性塌陷与其他折叠事件隔离开来。在没有竞争过程的情况下，我们直接测量了蛋白质疏水塌陷的动力学。塌陷是由激光诱导的简单蛋白质的酸变性形式的温度跃迁触发的，并通过置于蛋白质末端的探针之间的荧光共振能量转移进行监测。疏水塌陷的弛豫时间在305 K时仅为约60 ns，甚至比二级结构形成还要快。在更高的温度下，随着蛋白质在更强的疏水力作用下变得越来越致密，我们观察到崩溃动力学的减慢。这种动态疏水作用是理论上预测的动态玻璃化转变的高温类似物。我们的结果表明，在生理条件下，许多蛋白质会通过折叠成无结构的小球而开始折叠。推测局部运动将推动对塌陷小球中本机结构的后续搜索。

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