4.8 Review

Conformational freedom of metalloproteins revealed by paramagnetism-assisted NMR

Journal

COORDINATION CHEMISTRY REVIEWS
Volume 257, Issue 19-20, Pages 2652-2667

Publisher

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

Funding

  1. Ente Cassa di Risparmio
  2. MIUR-FIRB [RBLA032ZM7, RBRN07BMCT]
  3. European Commission [228461, 261572, 261863]

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.8
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available