4.6 Review

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

Journal

FEBS JOURNAL
Volume 278, Issue 5, Pages 704-715

Publisher

WILEY
DOI: 10.1111/j.1742-4658.2011.08005.x

Keywords

chemical shift mapping; NMR; NOE; protein; protein complex; protein dynamics; protein folding; protein interaction; protein mutagenesis; saturation difference

Funding

  1. Australian Research Council [DP0774245, DP0879065, DP1095728, DP110103161]
  2. Swiss National Science Foundation
  3. Australian Research Council [DP0879065] Funding Source: Australian Research Council

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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-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 multicomponent systems, as well as in the solid state and in vivo.

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