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Macromolecular NMR spectroscopy for the non‐spectroscopist: beyond macromolecular solution structure determination
Author(s) -
Bieri Michael,
Kwan Ann H.,
Mobli Mehdi,
King Glenn F.,
Mackay Joel P.,
Gooley Paul R.
Publication year - 2011
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2011.08005.x
Subject(s) - macromolecule , nuclear magnetic resonance spectroscopy , spectroscopy , chemistry , chemical physics , transverse relaxation optimized spectroscopy , molecular dynamics , range (aeronautics) , two dimensional nuclear magnetic resonance spectroscopy , affinities , solid state nuclear magnetic resonance , structural biology , nuclear magnetic resonance spectroscopy of nucleic acids , fluorine 19 nmr , computational chemistry , materials science , nuclear magnetic resonance , physics , stereochemistry , biochemistry , quantum mechanics , composite material
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 .