title: Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination.
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.
authors.affiliation: Department of Biochemistry and Molecular Biology, Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, Australia.
authors.forename: Michael
authors.initials: M
authors.lastname: Bieri
authors.forename: Ann H
authors.initials: AH
authors.lastname: Kwan
authors.forename: Mehdi
authors.initials: M
authors.lastname: Mobli
authors.forename: Glenn F
authors.initials: GF
authors.lastname: King
authors.forename: Joel P
authors.initials: JP
authors.lastname: Mackay
authors.forename: Paul R
authors.initials: PR
authors.lastname: Gooley
mesh_terms: D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D015394:Molecular Structure; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*
chemical_list: D011506:Proteins