Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination

被引:39
作者
Bieri, Michael [1 ]
Kwan, Ann H. [2 ]
Mobli, Mehdi [3 ]
King, Glenn F. [3 ]
Mackay, Joel P. [2 ]
Gooley, Paul R. [1 ]
机构
[1] Univ Melbourne, Mol Sci & Biotechnol Inst Bio21, Dept Biochem & Mol Biol, Parkville, Vic 3010, Australia
[2] Univ Sydney, Sch Mol Biosci, Sydney, NSW 2006, Australia
[3] Univ Queensland, Inst Mol Biosci, St Lucia, Qld, Australia
基金
澳大利亚研究理事会; 瑞士国家科学基金会;
关键词
chemical shift mapping; NMR; NOE; protein; protein complex; protein dynamics; protein folding; protein interaction; protein mutagenesis; saturation difference; RELAXATION DISPERSION NMR; SOLID-STATE NMR; NUCLEAR MAGNETIC-RESONANCE; MODEL-FREE APPROACH; ANGLE-SPINNING NMR; DIHYDROFOLATE-REDUCTASE CATALYSIS; PROTEIN-STRUCTURE DETERMINATION; LIGAND-BINDING; LIVING CELLS; BACKBONE DYNAMICS;
D O I
10.1111/j.1742-4658.2011.08005.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A strength of NMR spectroscopy is its ability to monitor, on an atomic level, molecular changes and interactions. In this review, which is intended for non-spectroscopists, we describe major uses of NMR in protein science beyond solution structure determination. After first touching on how NMR can be used to quickly determine whether a mutation induces structural perturbations in a protein, we describe the unparalleled ability of NMR to monitor binding interactions over a wide range of affinities, molecular masses and solution conditions. We discuss the use of NMR to measure the dynamics of proteins at the atomic level and over a wide range of timescales. Finally, we outline new and expanding areas such as macromolecular structure determination in multicomponent systems, as well as in the solid state and in vivo.
引用
收藏
页码:704 / 715
页数:12
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