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利用红边激发位移方法揭示溶剂弛豫动力学与蛋白质构象之间的关联。

Novel insights in linking solvent relaxation dynamics and protein conformations utilizing red edge excitation shift approach.

机构信息

Crystallography and Molecular Biology Division, Saha Institute of Nuclear Physics, Homi Bhabha National Institute, 1/AF Bidhannagar, Kolkata, India.

出版信息

Emerg Top Life Sci. 2021 May 14;5(1):89-101. doi: 10.1042/ETLS20200256.

DOI:10.1042/ETLS20200256
PMID:33416893
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7611131/
Abstract

Protein hydration dynamics plays an important role in many physiological processes since protein fluctuations, slow solvation, and the dynamics of hydrating water are all intrinsically related. Red edge excitation shift (REES) is a unique and powerful wavelength-selective (i.e. excitation-energy dependent) fluorescence approach that can be used to directly monitor the environment-induced restriction and dynamics around a polar fluorophore in a complex biological system. This review is mainly focused on recent applications of REES and a novel analysis of REES data to monitor the structural dynamics, functionally relevant conformational transitions and to unmask the structural ensembles in proteins. In addition, the novel utility of REES in imaging protein aggregates in a cellular context is discussed. We believe that the enormous potential of REES approach showcased in this review will engage more researchers, particularly from life sciences.

摘要

蛋白质水合动力学在许多生理过程中起着重要作用,因为蛋白质波动、缓慢的溶剂化以及水合水的动力学都与内在相关。红边激发位移(REES)是一种独特而强大的波长选择性(即激发能量依赖性)荧光方法,可用于直接监测复杂生物系统中极性荧光团周围环境诱导的限制和动力学。本综述主要集中于 REES 的最新应用,以及对 REES 数据的新分析,以监测结构动力学、功能相关构象转变,并揭示蛋白质中的结构集合体。此外,还讨论了 REES 在细胞环境中成像蛋白质聚集体的新应用。我们相信,本综述中展示的 REES 方法的巨大潜力将吸引更多的研究人员,特别是生命科学领域的研究人员。

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