溶液态核磁共振光谱与蛋白质折叠

Solution-state nuclear magnetic resonance spectroscopy and protein folding.

作者信息

Cabrita Lisa D, Waudby Christopher A, Dobson Christopher M, Christodoulou John

机构信息

Department of Structural and Molecular Biology, University College London, London, UK.

出版信息

Methods Mol Biol. 2011;752:97-120. doi: 10.1007/978-1-60327-223-0_7.

DOI:10.1007/978-1-60327-223-0_7

PMID:21713633

Abstract

A protein undergoes a variety of structural changes during its folding and misfolding and a knowledge of its behaviour is key to understanding the molecular details of these events. Solution-state NMR spectroscopy is unique in that it can provide both structural and dynamical information at both high-resolution and at a residue-specific level, and is particularly useful in the study of dynamic systems. In this chapter, we describe NMR strategies and how they are applied in the study of protein folding and misfolding.

摘要

一种蛋白质在折叠和错误折叠过程中会经历多种结构变化，了解其行为是理解这些事件分子细节的关键。溶液态核磁共振光谱具有独特性，因为它能够在高分辨率和残基特异性水平上提供结构和动力学信息，在动态系统研究中特别有用。在本章中，我们将描述核磁共振策略以及它们如何应用于蛋白质折叠和错误折叠的研究。