Coarse-grained Molecular Dynamics Simulations of Ca²⁺-Calmodulin

Calmodulin (CaM) is a primary Ca²⁺ signal transducer protein that undergoes multiple conformations upon Ca²⁺ binding, which allow it to bind and activate a myriad of target proteins. An appropriate force field to model the effect of Ca²⁺ on the dynamics of CaM is still lacking. Here, we present a coarse-grained approach using the Associative memory, Water mediated, Structure and Energy Model (AWSEM) force field to study the Ca²⁺-induced conformational changes on CaM. We have parameterized the force field for the Ca²⁺-CaM to match the experimental observables. This model provides mechanistic insights on CaM’s ability of target binding and selection.