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

by: Michael Bieri, Ann H. Kwan, Mehdi Mobli, Glenn F. King, Joel P. Mackay, Paul R. Gooley
FEBS Journal, Vol. 278, No. 5. (1 March 2011), pp. 704-715, doi:10.1111/j.1742-4658.2011.08005.x  Key: citeulike:8893345

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Abstract

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-spectroscopist, 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.


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