The effect of macromolecular crowding, ionic strength and calcium binding on calmodulin dynamics.

ABSTRACT: The flexibility in the structure of calmodulin (CaM) allows its binding to over 300 target proteins in the cell. To investigate the structure-function relationship of CaM, we combined methods of computer simulation and experiments based on circular dichroism (CD) to investigate the structural characteristics of CaM that influence its target recognition in crowded cell-like conditions. We developed a unique multiscale solution of charges computed from quantum chemistry, together with protein reconstruction, coarse-grained molecular simulations, and statistical physics, to represent the charge distribution in the transition from apoCaM to holoCaM upon calcium binding. Computationally, we found that increased levels of macromolecular crowding, in addition to calcium binding and ionic strength

SUBMITTER: Wang Q 

PROVIDER: S-EPMC3145654 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature