Conformational freedom of metalloproteins revealed by paramagnetism-assisted NMR
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- 作者：Marco Fragai ; Claudio Luchinat ; Giacomo Parigi ; Enrico Ravera
- 关键词：Paramagnetic NMR ; Multiple conformations ; Conformational heterogeneity ; Pseudocontact shifts ; Residual dipolar couplings ; Paramagnetic relaxation enhancements
- 刊名：Coordination Chemistry Reviews
- 出版年：2013
- 出版时间：October, 2013
- 年：2013
- 卷：257
- 期：19-20
- 页码：2652-2667
- 全文大小：4103 K
文摘
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.