Issue 25, 2012

Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins

Abstract

Multidomain proteins are often composed of rigid domains that can reorient in solution more or less freely. Calmodulin (CaM) is a two domain protein which can experience a large degree of conformational freedom thanks to a mobile linker connecting the N-terminal and C-terminal domains of the protein. The maximum occurrences (MOs) of the possible protein conformations have been analyzed using the paramagnetic relaxation enhancements (PREs) induced by a gadolinium(III) ion together with the paramagnetic pseudocontact shift and residual dipolar coupling restraints measured in the presence of terbium(III), thulium(III) or dysprosium(III) ions. The results suggest that the PREs provide complementary information useful for improving the description of the conformational heterogeneity of the protein. The data, acquired at 298 K and at 278 K, suggest that compact conformations are disfavoured by decreasing the temperature.

Graphical abstract: Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins

Supplementary files

Article information

Article type
Paper
Submitted
14 Jan 2012
Accepted
20 Apr 2012
First published
23 Apr 2012

Phys. Chem. Chem. Phys., 2012,14, 9149-9156

Paramagnetic relaxation enhancement for the characterization of the conformational heterogeneity in two-domain proteins

I. Bertini, C. Luchinat, M. Nagulapalli, G. Parigi and E. Ravera, Phys. Chem. Chem. Phys., 2012, 14, 9149 DOI: 10.1039/C2CP40139H

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