Structure-based protocol for identifying mutations that enhance protein-protein binding affinities.

ABSTRACT: The ability to manipulate protein binding affinities is important for the development of proteins as biosensors, industrial reagents, and therapeutics. We have developed a structure-based method to rationally predict single mutations at protein-protein interfaces that enhance binding affinities. The protocol is based on the premise that increasing buried hydrophobic surface area and/or reducing buried hydrophilic surface area will generally lead to enhanced affinity if large steric clashes are not introduced and buried polar groups are not left without a hydrogen bond partner. The procedure selects affinity enhancing point mutations at the protein-protein interface using three criteria: (1) the mutation must be from a polar amino acid to a non-polar amino acid or from a non-polar amino aci

SUBMITTER: Sammond DW 

PROVIDER: S-EPMC2682327 | biostudies-literature | 2007 Aug

REPOSITORIES: biostudies-literature