通过动态核磁共振光谱分析蛋白质-配体相互作用。

Analyzing protein-ligand interactions by dynamic NMR spectroscopy.

作者信息

Mittermaier Anthony, Meneses Erick

机构信息

Department of Chemistry, McGill University, Montreal, QC, Canada.

出版信息

Methods Mol Biol. 2013;1008:243-66. doi: 10.1007/978-1-62703-398-5_9.

DOI:10.1007/978-1-62703-398-5_9

PMID:23729255

Abstract

Nuclear magnetic resonance (NMR) spectroscopy can provide detailed information on protein-ligand interactions that is inaccessible using other biophysical techniques. This chapter focuses on NMR-based approaches for extracting affinity and rate constants for weakly binding transient protein complexes with lifetimes of less than about a second. Several pulse sequences and analytical techniques are discussed, including line-shape simulations, spin-echo relaxation dispersion methods (CPMG), and magnetization exchange (EXSY) experiments.

摘要

核磁共振（NMR）光谱能够提供关于蛋白质 - 配体相互作用的详细信息，而这些信息是其他生物物理技术无法获取的。本章重点介绍基于核磁共振的方法，用于提取寿命小于约一秒的弱结合瞬态蛋白质复合物的亲和力和速率常数。文中讨论了几种脉冲序列和分析技术，包括线形模拟、自旋回波弛豫色散方法（CPMG）以及磁化交换（EXSY）实验。