圆二色性及其在蛋白质折叠研究中的应用。

Circular dichroism and its use in protein-folding studies.

作者信息

Clarke David T

机构信息

Central Laser Facility, Science and Technology Facilities Council, Research Complex at Harwell, Rutherford Appleton Laboratory, Didcot, UK.

出版信息

Methods Mol Biol. 2011;752:59-72. doi: 10.1007/978-1-60327-223-0_5.

DOI:10.1007/978-1-60327-223-0_5

PMID:21713631

Abstract

The way in which proteins fold into the complex 3 dimensional structures that are responsible for their function is a subject of great practical as well as fundamental significance because of the involvement of folding and misfolding in a number of serious human and animal diseases. Ultraviolet circular dichroism (CD) reports on the secondary and tertiary structure of proteins. Measurements can be made on proteins in the solution phase, and critically time-resolved measurements can be made with millisecond resolution. This combination of characteristics makes CD a useful tool for investigating protein folding, and indeed any process involving changes in protein structure. Experimental methods for a typical time-resolved CD experiment are described, and some common problems identified.

摘要

蛋白质折叠成负责其功能的复杂三维结构的方式，由于折叠和错误折叠与许多严重的人类和动物疾病有关，因此具有重大的实际意义和基础意义。紫外圆二色性（CD）可反映蛋白质的二级和三级结构。可以对溶液状态的蛋白质进行测量，并且关键的是，可以以毫秒分辨率进行时间分辨测量。这些特性的结合使CD成为研究蛋白质折叠以及任何涉及蛋白质结构变化过程的有用工具。本文描述了典型时间分辨CD实验的实验方法，并指出了一些常见问题。