Thermodynamic coupling between neighboring binding sites in homo-oligomeric ligand sensing proteins from mass resolved ligand-dependent population distributions.

ABSTRACT: Homo-oligomeric ligand-activated proteins are ubiquitous in biology. The functions of such molecules are commonly regulated by allosteric coupling between ligand-binding sites. Understanding the basis for this regulation requires both quantifying the free energy ΔG transduced between sites, and the structural basis by which it is transduced. We consider allostery in three variants of the model ring-shaped homo-oligomeric trp RNA-binding attenuation protein (TRAP). First, we developed a nearest-neighbor statistical thermodynamic binding model comprising microscopic free energies for ligand binding to isolated sites ΔG₀ , and for coupling between adjacent sites, ΔG_α . Using the resulting partition function (PF) we explored the effects of these parameters on simulated po

SUBMITTER: Li W 

PROVIDER: S-EPMC9514064 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature