Experimental library screening demonstrates the successful application of computational protein design to large structural ensembles.

ABSTRACT: The stability, activity, and solubility of a protein sequence are determined by a delicate balance of molecular interactions in a variety of conformational states. Even so, most computational protein design methods model sequences in the context of a single native conformation. Simulations that model the native state as an ensemble have been mostly neglected due to the lack of sufficiently powerful optimization algorithms for multistate design. Here, we have applied our multistate design algorithm to study the potential utility of various forms of input structural data for design. To facilitate a more thorough analysis, we developed new methods for the design and high-throughput stability determination of combinatorial mutation libraries based on protein design calculations. The applicatio

SUBMITTER: Allen BD 

PROVIDER: S-EPMC2993350 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature