Calmodulin Pathway

Understanding the EF-hand closing pathway using non-biased interatomic

potentials

L. Dupuis and Normand Mousseau

Citation: J. Chem. Phys. 136, 035101 (2012); doi: 10.1063/1.3671986

View online: http://dx.doi.org/10.1063/1.3671986

View Table of Contents: http://jcp.aip.org/resource/1/JCPSA6/v136/i3

Published by the American Institute of Physics.

Additional information on J. Chem. Phys.

Journal Homepage: http://jcp.aip.org/

Journal Information: http://jcp.aip.org/about/about_the_journal

Top downloads: http://jcp.aip.org/features/most_downloaded

Information for Authors: http://jcp.aip.org/authors

Downloaded 15 May 2012 to 132.252.243.10. Redistribution subject to AIP license or copyright; see http://jcp.aip.org/about/rights_and_permissions

THE JOURNAL OF CHEMICAL PHYSICS 136, 035101 (2012)

Understanding the EF-hand closing pathway using non-biased

interatomic potentials

L. Dupuis1 and Normand Mousseau2,a)

1

Département de Biochimie, Centre Robert-Cedergren and GEPROM, Université de Montréal,

C.P. 6128, Succursale Centre-Ville, Montréal, Québec H3C 3J7, Canada

2

Département de Physique, Centre Robert-Cedergren and GEPROM, Université de Montréal,

C.P. 6128, Succursale Centre-Ville, Montréal, Québec H3C 3J7, Canada

(Received 3 August 2011; accepted 4 December 2011; published online 17 January 2012)

The EF-hand superfamily of proteins is characterized by the presence of calcium binding helix-loophelix structures. Many of these proteins undergo considerable motion responsible for a wide range of

properties upon binding but the exact mechanism at the root of this motion is not fully understood.

Here, we use an unbiased accelerated multiscale simulation scheme, coupled with two force fields

— CHARMM-EEF1 and the extended OPEP — to explore in details the closing pathway, from the

unbound holo state to the closed apo state, of two EF-hand proteins, the Calmodulin and Troponin

C N-terminal nodules. Based on a number of closing...