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探究单分子蛋白质构象动力学。

Probing single-molecule protein conformational dynamics.

作者信息

Lu H Peter

机构信息

Pacific Northwest National Laboratory, Fundamental Science Division, P.O. Box 999, Richland, Washington 99352, USA.

出版信息

Acc Chem Res. 2005 Jul;38(7):557-65. doi: 10.1021/ar0401451.

Abstract

Protein conformational fluctuations and dynamics, often complex and associated with inhomogeneities, play a crucial role in biomolecular functions. It is extremely difficult to characterize such inhomogeneous dynamics in an ensemble-averaged measurement, especially when the proteins are involved in multiple-step, multiple-conformation complex chemical interactions and transformations, such as in enzymatic reactions, protein-protein interactions, and ion-channel membrane protein processes. Alternatively, single-molecule spectroscopy is a powerful approach to probing and analyzing protein conformational dynamics in real time.

摘要

蛋白质构象波动和动力学通常很复杂且与不均匀性相关,在生物分子功能中起着关键作用。在总体平均测量中表征这种不均匀动力学极其困难,尤其是当蛋白质参与多步、多构象的复杂化学相互作用和转变时,例如在酶促反应、蛋白质 - 蛋白质相互作用和离子通道膜蛋白过程中。另外,单分子光谱学是实时探测和分析蛋白质构象动力学的有力方法。

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