Chloride Binding in Trimeric Coiled Coils: Free Energy and Structural Determinants from Molecular Simulations.

ABSTRACT: Coiled coils, owing to their simple yet versatile architecture, serve as valuable model systems for both experimental and computational studies in protein science. Whereas the sequence-structure relationships that govern their oligomeric state and stability have been thoroughly investigated, important gaps remain, most notably regarding the role of central chloride ions coordinated by asparagine triads observed in several trimeric coiled-coil (TCC) crystal structures. To investigate the thermodynamics of chloride binding at this site, we performed extensive molecular simulations using metadynamics and alchemical free-energy calculations, both enhanced with replica exchange, to determine the chloride binding free energy (ΔG_bind) in three TCCs of similar length but differen

SUBMITTER: Nifosi R 

PROVIDER: S-EPMC12933892 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature