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. © 2011 FEBS.
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Bieri, M., Kwan, A. H., Mobli, M., King, G. F., MacKay, J. P., & Gooley, P. R. (2011, March). Macromolecular NMR spectroscopy for the non-spectroscopist: Beyond macromolecular solution structure determination. FEBS Journal. https://doi.org/10.1111/j.1742-4658.2011.08005.x
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