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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Continuous dissolution of structure during the unfolding of a small protein
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Continuous dissolution of structure during the unfolding of a small protein

机译：小蛋白展开过程中结构的持续溶解

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The unfolding kinetics of many small proteins appears to be first order, when measured by ensemble-averaging probes such as fluorescence and circular dichroism. For one such protein, monellin, it is shown here that hidden behind this deceptive simplicity is a complexity that becomes evident with the use of experimental probes that are able to discriminate between different conformations in an ensemble of structures. In this study, the unfolding of monellin has been probed by measurement of the changes in the distributions of 4 different intramolecular distances, using a mul-tisite, time-resolved fluorescence resonance energy transfer methodology. During the course of unfolding, the protein molecules are seen to undergo slow and continuous, diffusive swelling. The swelling process can be modeled as the slow diffusive swelling of a Rouse-like chain with some additional noncovalent, intramolecular interactions. Here, we show that specific structure is lost during the swelling process gradually, and not in an all-or-none manner, during unfolding.
机译：当用整体平均探针（例如荧光和圆二色性）测量时，许多小蛋白质的展开动力学似乎是一阶的。对于一种这样的蛋白质，monellin，在此表明，这种欺骗性简单性背后隐藏着一种复杂性，这种复杂性通过使用能够区分结构整体中不同构象的实验探针而变得显而易见。在这项研究中，通过使用多种时间分辨的荧光共振能量转移方法，通过测量4种不同分子内距离的分布变化来探测莫奈菌素的展开。在展开过程中，发现蛋白质分子经历缓慢而连续的扩散性溶胀。可以将溶胀过程建模为具有一些其他非共价分子内相互作用的Rouse样链的缓慢扩散溶胀。在这里，我们显示出在展开过程中，特定的结构逐渐消失，而不是完全消失。

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