Review
High-resolution solid-state MAS NMR of proteins—Crh as an example
Article first published online: 17 DEC 2007
DOI: 10.1002/mrc.2106
Copyright © 2007 John Wiley & Sons, Ltd.
Issue
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Magnetic Resonance in Chemistry
Special Issue: New techniques in solid-state NMR
Volume 45, Issue S1, pages S24–S31, December 2007
Additional Information
How to Cite
Böckmann, A. (2007), High-resolution solid-state MAS NMR of proteins—Crh as an example. Magn. Reson. Chem., 45: S24–S31. doi: 10.1002/mrc.2106
Publication History
- Issue published online: 21 DEC 2007
- Article first published online: 17 DEC 2007
- Manuscript Accepted: 12 SEP 2007
- Manuscript Revised: 4 SEP 2007
- Manuscript Received: 15 JUN 2007
Funded by
- CNRS. Grant Number: PICS no 2424
- French Research Ministry (ACI Biologie Cellulaire Moléculaire et Structurale 2003)
- ANR. Grant Number: JCJC 2005
- CNRS. Grant Number: PICS no 2424
- The French Research Ministry (ACI Biologie Cellulaire Moléculaire et Structurale 2003)
- ANR. Grant Number: JCJC 2005
- Abstract
- References
- Cited By
Keywords:
- NMR 1H;
- 13C;
- 15N;
- protein;
- magic angle spinning;
- microcrystalline;
- solid-state NMR
Abstract
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 [13C,15N]-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.

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