STD-NMR: application to transient interactions between biomolecules-a quantitative approach

被引:136
作者
Angulo, Jesus [1 ]
Nieto, Pedro M. [1 ]
机构
[1] CSIC US, Inst Invest Quim, Seville 41092, Spain
来源
EUROPEAN BIOPHYSICS JOURNAL WITH BIOPHYSICS LETTERS | 2011年 / 40卷 / 12期
关键词
NMR spectroscopy; Saturation transfer difference NMR (STD NMR) spectroscopy; Molecular recognition; Receptor-ligand interactions; TRANSFER DIFFERENCE NMR; MATRIX CORCEMA ANALYSIS; VIRUS-LIKE PARTICLES; SATURATION-TRANSFER; LIGAND-BINDING; MOLECULAR RECOGNITION; DIHYDROFOLATE-REDUCTASE; PROTEIN INTERACTIONS; COMPLETE RELAXATION; SUGAR-OLIGOAMIDES;
D O I
10.1007/s00249-011-0749-5
中图分类号
Q6 [生物物理学];
学科分类号
071011 [生物物理学];
摘要
Saturation transfer difference NMR (STD NMR) spectroscopy is one of the most powerful NMR techniques for detection and characterization of transient (fast) receptor-ligand interactions in solution. By observing the signals of a small molecule (ligand) with spectroscopic properties suitable for high-resolution studies, irrespective of receptor size, STD NMR enables quantitative structural and affinity information to be obtained about the molecular recognition process under study. Approximately one decade after its introduction, the technique has reached maturity, and is highly robust and useful. The objective of this article is to review the current status of this powerful technique, with particular emphasis on quantitative applications, within the framework of the (bio-)chemistry of molecular recognition.
引用
收藏
页码:1357 / 1369
页数:13
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