Energy landscape views for interplays among folding, binding, and allostery of calmodulin domains.

ABSTRACT: Ligand binding modulates the energy landscape of proteins, thus altering their folding and allosteric conformational dynamics. To investigate such interplay, calmodulin has been a model protein. Despite much attention, fully resolved mechanisms of calmodulin folding/binding have not been elucidated. Here, by constructing a computational model that can integrate folding, binding, and allosteric motions, we studied in-depth folding of isolated calmodulin domains coupled with binding of two calcium ions and associated allosteric conformational changes. First, mechanically pulled simulations revealed coexistence of three distinct conformational states: the unfolded, the closed, and the open states, which is in accord with and augments structural understanding of recent single-molecule experime

SUBMITTER: Li W 

PROVIDER: S-EPMC4115553 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature