| Literature DB >> 21214861 |
Michael Bieri1, Ann H Kwan, Mehdi Mobli, Glenn F King, Joel P Mackay, Paul R Gooley.
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.Mesh:
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Year: 2011 PMID: 21214861 DOI: 10.1111/j.1742-4658.2011.08005.x
Source DB: PubMed Journal: FEBS J ISSN: 1742-464X Impact factor: 5.542