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.

Conformational freedom of metalloproteins revealed by paramagnetism-assisted NMR / Marco Fragai;Claudio Luchinat;Giacomo Parigi;Enrico Ravera. - In: COORDINATION CHEMISTRY REVIEWS. - ISSN 0010-8545. - STAMPA. - 257(2013), pp. 2652-2667. [10.1016/j.ccr.2013.02.009]

Conformational freedom of metalloproteins revealed by paramagnetism-assisted NMR

FRAGAI, MARCO;LUCHINAT, CLAUDIO;PARIGI, GIACOMO;RAVERA, ENRICO
2013

Abstract

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.
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Marco Fragai;Claudio Luchinat;Giacomo Parigi;Enrico Ravera
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2158/803283
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