Journal
COORDINATION CHEMISTRY REVIEWS
Volume 257, Issue 19-20, Pages 2652-2667Publisher
ELSEVIER SCIENCE SA
DOI: 10.1016/j.ccr.2013.02.009
Keywords
Paramagnetic NMR; Multiple conformations; Conformational heterogeneity; Pseudocontact shifts; Residual dipolar couplings; Paramagnetic relaxation enhancements
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Funding
- Ente Cassa di Risparmio
- MIUR-FIRB [RBLA032ZM7, RBRN07BMCT]
- European Commission [228461, 261572, 261863]
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In many biologically relevant cases protein-ligand or protein-protein recognition occurs thanks to the availability of multiple conformational states of at least one of the partners. Paramagnetism-assisted NMR is a powerful tool to address the conformational freedom of proteins. Appropriate experiments and theoretical interpretation permit the characterization of biologically relevant protein-protein interactions in solution. The paradigmatic examples of two-domain metalloproteins such as calmodulin (CaM) or two-domain metalloenzymes such as matrix metalloproteinases (MMP) are discussed. (C) 2013 Elsevier B.V. All rights reserved.
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