Gabriel Rocklin
University of Washington
Molecular Engineering of Sciences

"Designing protein structures de novo the Rosetta way"
Many natural signaling molecules and toxins are small proteins (50 residues) with multiple disulfide linkages, endowing them wih high stability and protease resistance. Rationally designing this class of proteins probes the limits of design methods and may also generate useful scaffolds for introducing binding functionality. Using Rosetta, we are attempting to design small, disulfide-rich proteins de novo; in other words, using completely novel computationally generated backbones.  I will describe background on the Rosetta design process and early progress toward designing disulfide-linked proteins with a miniaturized version of the Protein G fold.

Gabe is a postdoctoral researcher in Dave Baker's lab designing de novo protein structures that can bind to interesting targets. Gabe studied protein-ligand binding affinities with Ken Dill.