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Using chemical shift perturbation to characterise ligand binding

Published:2013-08 Issue: Volume:73 Page:1-16
ISSN:0079-6565
Container-title:Progress in Nuclear Magnetic Resonance Spectroscopy
language:en
Short-container-title:Progress in Nuclear Magnetic Resonance Spectroscopy

Author:

Williamson Mike P.

Publisher

Elsevier BV

Reference107 articles.

1. Mapping protein-protein interactions in solution by NMR spectroscopy;Zuiderweg;Biochemistry,2002

2. Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution;Pervushin;Proc. Natl. Acad. Sci. USA,1997

3. Isotopically discriminated NMR spectroscopy: a tool for investigating complex protein interactions in vitro;Golovanov;J. Am. Chem. Soc.,2007

4. Spatial localization of ligand binding sites from electron current density surfaces calculated from NMR chemical shift perturbations;McCoy;J. Am. Chem. Soc.,2002

5. Discovering high-affinity ligands for proteins: SAR by NMR;Shuker;Science,1996

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