Sweeping away protein aggregation with entropic bristles: intrinsically disordered protein fusions enhance soluble expression.

ABSTRACT: Intrinsically disordered, highly charged protein sequences act as entropic bristles (EBs), which, when translationally fused to partner proteins, serve as effective solubilizers by creating both a large favorable surface area for water interactions and large excluded volumes around the partner. By extending away from the partner and sweeping out large molecules, EBs can allow the target protein to fold free from interference. Using both naturally occurring and artificial polypeptides, we demonstrate the successful implementation of intrinsically disordered fusions as protein solubilizers. The artificial fusions discussed herein have a low level of sequence complexity and a high net charge but are diversified by means of distinctive amino acid compositions and lengths. Using 6xHis fusions a

SUBMITTER: Santner AA 

PROVIDER: S-EPMC4141500 | biostudies-literature | 2012 Sep

REPOSITORIES: biostudies-literature