Abstract 1292 Employing Solution Characterization to Understand Calmodulin Complexes with Target Enzyme Peptides

Calmodulin (CaM) plays a crucial role in Ca2+-dependent signal transduction. When Ca2+ binds to CaM, it induces a conformational change that creates a hydrophobic patch essential for interacting with the calmodulin-binding domain (CaMBD) of target proteins. The structures of the CaM/CMBD complex can be categorized into extended and collapsed models, with stoichiometry ranging from 1 to 2 CMBD, which reflecting the hydrodynamic property of CaM. Despite decades of efforts, the model of this complex remains to be elucidated solely through structural determination.