Computational Design of the β-Sheet Surface of a Red Fluorescent Protein Allows Control of Protein Oligomerization.

ABSTRACT: Computational design has been used with mixed success for the design of protein surfaces, with directed evolution heretofore providing better practical solutions than explicit design. Directed evolution, however, requires a tractable high-throughput screen because the random nature of mutation does not enrich for desired traits. Here we demonstrate the successful design of the β-sheet surface of a red fluorescent protein (RFP), enabling control over its oligomerization. To isolate the problem of surface design, we created a hybrid RFP from DsRed and mCherry with a stabilized protein core that allows for monomerization without loss of fluorescence. We designed an explicit library for which 93 of 96 (97%) of the protein variants are soluble, stably fluorescent, and monomeric. RFPs are heavil

SUBMITTER: Wannier TM 

PROVIDER: S-EPMC4468108 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature