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High‐resolution solid‐state MAS NMR of proteins—Crh as an example
Author(s) -
Böckmann Anja
Publication year - 2007
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.2106
Subject(s) - chemistry , solid state nuclear magnetic resonance , magic angle spinning , microcrystalline , nuclear magnetic resonance spectroscopy , macromolecule , folding (dsp implementation) , chemical physics , computational chemistry , crystallography , nuclear magnetic resonance , stereochemistry , biochemistry , physics , electrical engineering , engineering
Solid‐state NMR spectroscopy provides unique possibilities for the structural investigation of insoluble molecules at the atomic level. Recent efforts aim at solving the complete structures of biological macromolecules using high‐resolution magic angle spinning NMR. Structurally homogenous samples of [ 13 C, 15 N]‐labeled proteins have to be used in this type of studies. Microcrystalline model proteins present valuable tools for the developments of methods towards this goal. This review discusses recent progress in the field, using the Crh protein as an illustrative example. We discuss strategies for resonance assignments and for the determination of structure and dynamics, as well as techniques for the detection of protein interaction partners and folding mechanisms by solid‐state NMR methods. Copyright © 2007 John Wiley & Sons, Ltd.