Ligand Binding Introduces Significant Allosteric Shifts in the Locations of Protein Fluctuations.

ABSTRACT: Allostery is usually considered to be a mechanism for transmission of signals associated with physical or dynamic changes in some part of a protein. Here, we investigate the changes in fluctuations across the protein upon ligand binding based on the fluctuations computed with elastic network models. These results suggest that binding reduces the fluctuations at the binding site but increases fluctuations at remote sites, but not to fully compensating extents. If there were complete conservation of entropy, then only the enthalpies of binding would matter and not the entropies; however this does not appear to be the case. Experimental evidence also suggests that energies and entropies of binding can compensate but that the extent of compensation varies widely from case to case. Our results

SUBMITTER: Kumar A 

PROVIDER: S-EPMC8440829 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature