Ontology highlight
ABSTRACT:
SUBMITTER: Huang PS
PROVIDER: S-EPMC4684731 | biostudies-literature | 2016 Jan
REPOSITORIES: biostudies-literature
Nature chemical biology 20151123 1
Despite efforts for over 25 years, de novo protein design has not succeeded in achieving the TIM-barrel fold. Here we describe the computational design of four-fold symmetrical (β/α)8 barrels guided by geometrical and chemical principles. Experimental characterization of 33 designs revealed the importance of side chain-backbone hydrogen bonds for defining the strand register between repeat units. The X-ray crystal structure of a designed thermostable 184-residue protein is nearly identical to th ...[more]