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

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

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

FEBS J. 2011 Jan 7;

Authors: Bieri M, Kwan AH, Mobli M, King GF, Mackay JP, Gooley PR

A strength of NMR spectroscopy is its ability to monitor, on an atomic level, molecular changes and interactions. In this article, 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 multi-component systems as well as in the solid state and in vivo.

PMID: 21214861 [PubMed - as supplied by publisher]



Source: PubMed
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