Retrospective study for the universal applicability of the residue-based linear free energy relationship in the two-state exchange of protein molecules.

ABSTRACT: Multiprobe measurements, such as NMR and hydrogen exchange studies, can provide the equilibrium constant, K, and rate constants for forward and backward processes, k and k', of the two-state structural changes of a polypeptide on a per-residue basis. We previously found a linear relationship between log K and log k and between log K and log k' for the topological exchange of a 27-residue bioactive peptide. To test the general applicability of the residue-based linear free energy relationship (rbLEFR), we performed a literature search to collect residue-specific K, k, and k' values in various exchange processes, including folding-unfolding equilibrium, coupled folding and binding of intrinsically disordered peptides, and structural fluctuations of folded proteins. The good linearity in a su

SUBMITTER: Fujinami D 

PROVIDER: S-EPMC9546931 | biostudies-literature | 2022 Oct

REPOSITORIES: biostudies-literature