Progress in correlation spectroscopy at ultra-fast magic-angle spinning: Basic building blocks and complex experiments for the study of protein structure and dynamics

被引:60
作者
Demers, Jean-Philippe [1 ]
Chevelkov, Veniamin [1 ]
Lange, Adam [1 ]
机构
[1] Max Planck Inst Biophys Chem, Dept NMR Based Struct Biol, D-37077 Gottingen, Germany
基金
加拿大自然科学与工程研究理事会;
关键词
Solid-state NMR; Protein structure; Protein dynamics; Ultra-fast magic-angle spinning; Paramagnetic proteins; SOLID-STATE NMR; NUCLEAR-MAGNETIC-RESONANCE; CROSS-POLARIZATION; ADIABATIC-PASSAGE; ROTATING SOLIDS; SENSITIVITY ENHANCEMENT; CHEMICAL-SHIFT; MICROCRYSTALLINE PROTEIN; DISTANCE MEASUREMENTS; LATTICE-RELAXATION;
D O I
10.1016/j.ssnmr.2011.07.002
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
Recent progress in multi-dimensional solid-state NMR correlation spectroscopy at high static magnetic fields and ultra-fast magic-angle spinning is discussed. A focus of the review is on applications to protein resonance assignment and structure determination as well as on the characterization of protein dynamics in the solid state. First, the consequences of ultra-fast spinning on sensitivity and sample heating are considered. Recoupling and decoupling techniques at ultra-fast MAS are then presented, as well as more complex experiments assembled from these basic building blocks. Furthermore, we discuss new avenues in biomolecular solid-state NMR spectroscopy that become feasible in the ultra-fast spinning regime, such as sensitivity enhancement based on paramagnetic doping, and the prospect of direct proton detection. (C) 2011 Elsevier Inc. All rights reserved.
引用
收藏
页码:101 / 113
页数:13
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