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用于研究蛋白质-配体相互作用的圆二色光谱法。

Circular dichroism spectroscopy for the study of protein-ligand interactions.

作者信息

Rodger Alison, Marrington Rachel, Roper David, Windsor Stuart

机构信息

Department of Chemistry, University of Warwick, Coventry, UK.

出版信息

Methods Mol Biol. 2005;305:343-64. doi: 10.1385/1-59259-912-5:343.

Abstract

Circular dichroism (CD) is the difference in absorption of left and right circularly polarized light, usually by a solution containing the molecules of interest. A signal is only measured for chiral molecules such as proteins. A CD spectrum provides information about the bonds and structures responsible for this chirality. When a small molecule (or ligand) binds to a protein, it acquires an induced CD (ICD) spectrum through chiral perturbation to its structure or electron rearrangements. The wavelengths of this ICD are determined by the ligand's own absorption spectrum, and the intensity of the ICD spectrum is determined by the strength and geometry of its interaction with the protein. Thus, ICD can be used to probe the binding of ligands to proteins. This chapter outlines protein CD and ICD, together with some of the issues relating to experimental design and implementation.

摘要

圆二色性(CD)是左旋和右旋圆偏振光吸收的差异,通常由含有感兴趣分子的溶液产生。只有手性分子(如蛋白质)才能测量到信号。CD光谱提供了有关导致这种手性的化学键和结构的信息。当小分子(或配体)与蛋白质结合时,它会通过对其结构的手性扰动或电子重排获得诱导CD(ICD)光谱。这种ICD的波长由配体自身的吸收光谱决定,而ICD光谱的强度则由其与蛋白质相互作用的强度和几何结构决定。因此,ICD可用于探测配体与蛋白质的结合。本章概述了蛋白质CD和ICD,以及一些与实验设计和实施相关的问题。

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