De Novo Proteins with Life-Sustaining Functions Are Structurally Dynamic.

ABSTRACT: Designing and producing novel proteins that fold into stable structures and provide essential biological functions are key goals in synthetic biology. In initial steps toward achieving these goals, we constructed a combinatorial library of de novo proteins designed to fold into 4-helix bundles. As described previously, screening this library for sequences that function in vivo to rescue conditionally lethal mutants of Escherichia coli (auxotrophs) yielded several de novo sequences, termed SynRescue proteins, which rescued four different E. coli auxotrophs. In an effort to understand the structural requirements necessary for auxotroph rescue, we investigated the biophysical properties of the SynRescue proteins, using both computational and experimental approaches. Results from circular dich

SUBMITTER: Murphy GS 

PROVIDER: S-EPMC4744525 | biostudies-literature | 2016 Jan

REPOSITORIES: biostudies-literature