Concentration-dependent thermodynamic analysis of the partition process of small ligands into proteins.

ABSTRACT: In the category of functional low-affinity interactions, small ligands may interact with multiple protein sites in a highly degenerate manner. Better conceived as a partition phenomenon at the molecular interface of proteins, such low-affinity interactions appear to be hidden to our current experimental resolution making their structural and functional characterization difficult in the low concentration regime of physiological processes. Characterization of the partition phenomenon under higher chemical forces could be a relevant strategy to tackle the problem provided the results can be scaled back to the low concentration range. Far from being trivial, such scaling demands a concentration-dependent understanding of self-interactions of the ligands, structural perturbations of the protein

SUBMITTER: Cirqueira L 

PROVIDER: S-EPMC9468351 | biostudies-literature | 2022

REPOSITORIES: biostudies-literature