Spatiotemporal correlations in denatured proteins: The dependence of fluorescence resonance energy transfer (FRET)-derived protein reconfiguration times on the location of the FRET probes.-猫眼课题宝

变性蛋白质的时空相关性：荧光共振能量转移 (FRET) 衍生的蛋白质重构时间对 FRET 探针位置的依赖性。

DOI：

发表时间：

2010

期刊：

Journal of Chemical Physics

影响因子：

4.4

通讯作者：

中科院分区：

化学2区

文献类型：

作者：

D. Makarov

为了了解变性蛋白质构象重构的固有时间尺度，人们付出了相当大的努力。然而，即使是简单的均聚物，也会表现出波动时间尺度的频谱，而不是独特的特征时间。因此，可以通过不同的测量来探测不同的时间尺度。受最近单分子荧光共振能量转移实验的启发，我从理论上研究了未折叠多肽内两个残基之间的距离波动所表现出的特征时间尺度如何取决于残基对的选择。通常发现随着残基之间的序列间隔减少，该时间尺度变得更短。然而，最大重构时间并不对应于位于链末端的残基，而是对应于距末端较短长度的每个残基。将这些发现与最近的单分子测量结果进行比较表明，后者可能具有瞬时残留结构的特征。

There has been considerable effort to understand the inherent time scale for conformational reconfiguration of denatured proteins. Even a simple homopolymer, however, exhibits a spectrum of fluctuation time scales rather than a unique characteristic time. Consequently, different time scales may be probed by different measurements. Motivated by recent single-molecule fluorescence resonance energy transfer experiments, here I have studied theoretically how the characteristic time scale exhibited by fluctuations of the distance between two residues within an unfolded polypeptide depends on the choice of the residue pair. This time scale was generally found to become shorter as the sequence separation between the residues is reduced. The maximum reconfiguration time, however, corresponds not to the residues being located at the ends of the chain but rather to each residue residing a short length apart from the ends. Comparison of these findings with recent single-molecule measurements suggests that the latter may bear signatures of transient residual structure.