GADIS: Algorithm for designing sequences to achieve target secondary structure profiles of intrinsically disordered proteins.

ABSTRACT: Many intrinsically disordered proteins (IDPs) participate in coupled folding and binding reactions and form alpha helical structures in their bound complexes. Alanine, glycine, or proline scanning mutagenesis approaches are often used to dissect the contributions of intrinsic helicities to coupled folding and binding. These experiments can yield confounding results because the mutagenesis strategy changes the amino acid compositions of IDPs. Therefore, an important next step in mutagenesis-based approaches to mechanistic studies of coupled folding and binding is the design of sequences that satisfy three major constraints. These are (i) achieving a target intrinsic alpha helicity profile; (ii) fixing the positions of residues corresponding to the binding interface; and (iii) maintaining th

SUBMITTER: Harmon TS 

PROVIDER: S-EPMC5001138 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature