Computational design of ligand-binding proteins with high affinity and selectivity.

ABSTRACT: The ability to design proteins with high affinity and selectivity for any given small molecule is a rigorous test of our understanding of the physiochemical principles that govern molecular recognition. Attempts to rationally design ligand-binding proteins have met with little success, however, and the computational design of protein-small-molecule interfaces remains an unsolved problem. Current approaches for designing ligand-binding proteins for medical and biotechnological uses rely on raising antibodies against a target antigen in immunized animals and/or performing laboratory-directed evolution of proteins with an existing low affinity for the desired ligand, neither of which allows complete control over the interactions involved in binding. Here we describe a general computational me

SUBMITTER: Tinberg CE 

PROVIDER: S-EPMC3898436 | biostudies-literature | 2013 Sep

REPOSITORIES: biostudies-literature