Intrinsic protein disorder uncouples affinity from binding specificity.

ABSTRACT: Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDRs) of proteins often function by molecular recognition, in which they undergo induced folding. Based on prior generalizations, the idea prevails in the IDP field that due to the entropic penalty of induced folding, the major functional advantage associated with this binding mode is "uncoupling" specificity from binding strength. Nevertheless, both weaker binding and high specificity of IDPs/IDRs rest on limited experimental observations, making these assumptions more speculations than evidence-supported facts. The issue is also complicated by the rather vague concept of specificity that lacks an exact measure, such as the K_d for binding strength. We addressed these issues by creating and analyzing

SUBMITTER: Lazar T 

PROVIDER: S-EPMC9601785 | biostudies-literature | 2022 Nov

REPOSITORIES: biostudies-literature