Mechanisms of noncanonical binding dynamics in multivalent protein-protein interactions.

ABSTRACT: Protein multivalency can provide increased affinity and specificity relative to monovalent counterparts, but these emergent biochemical properties and their mechanistic underpinnings are difficult to predict as a function of the biophysical properties of the multivalent binding partners. Here, we present a mathematical model that accurately simulates binding kinetics and equilibria of multivalent protein-protein interactions as a function of the kinetics of monomer-monomer binding, the structure and topology of the multidomain interacting partners, and the valency of each partner. These properties are all experimentally or computationally estimated a priori, including approximating topology with a worm-like chain model applicable to a variety of structurally disparate systems, thus making

SUBMITTER: Errington WJ 

PROVIDER: S-EPMC6926015 | biostudies-literature | 2019 Dec

REPOSITORIES: biostudies-literature