The free energy folding penalty accompanying binding of intrinsically disordered α-helical motifs.

ABSTRACT: Intrinsically disordered proteins (IDPs) are abundant in eukaryotic proteomes and preform critical roles in many cellular processes, most often through the association with globular proteins. Despite lacking a stable three-dimensional structure by themselves, they may acquire a defined conformation upon binding globular targets. The most common type of secondary structure acquired by these binding motifs entails formation of an α-helix. It has been hypothesized that such disorder-to-order transitions are associated with a significant free energy penalty due to IDP folding, which reduces the overall IDP-target affinity. However, the exact magnitude of IDP folding penalty in α-helical binding motifs has not been systematically estimated. Here, we report the folding penalty contributions for

SUBMITTER: Hadzi S 

PROVIDER: S-EPMC9202546 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature