NMR studies of weak protein-protein interactions

被引:14
|
作者
Lian, Lu-Yun [1 ]
机构
[1] Univ Liverpool, Inst Integrat Biol, NMR Ctr Struct Biol, Liverpool L69 7ZB, Merseyside, England
关键词
NMR; Weak; Protein; Interactions; Dissociation constants; PARAMAGNETIC RELAXATION ENHANCEMENT; ELECTRON-TRANSFER COMPLEX; CYTOCHROME-C PEROXIDASE; STRUCTURAL BASIS; DIPOLAR COUPLINGS; CROSS-SATURATION; REDOX PROTEINS; BINDING; RECOGNITION; DYNAMICS;
D O I
10.1016/j.pnmrs.2012.11.002
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
A study was conducted to demonstrate how nuclear magnetic resonance (NMR) was used to investigate weak heterotypic protein-protein interactions in which complexes were formed between different proteins rather the homotypic interactions which led to the multimerization of a particular protein. The study described methods for preparing weak protein complexes for NMR studies, and included the different types of isotope labeling required for the investigations along with as the practicalities of making protein-protein complexes that were functionally relevant. Different techniques were also used in the 'titration' mode in investigations of weak interactions where the NMR characteristics were observed as a function of increasing concentrations of a partner protein rather than as a single equilibrium mix with only one protein: protein concentration ratio.
引用
收藏
页码:59 / 72
页数:14
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