Lead Principal Investigators: Jack Greenblatt, Andrew Emili, Alexander Iakounine, Cheryl Arrowsmith, Aled Edwards
Our Structural Proteomics & Protein Dynamics effort involves two large sub-projects. The first utilizes affinity chromatography and complementary in vivo assays to discover protein complexes involving membrane proteins in yeast. Having finished the characterization of soluble yeast protein complexes, the Greenblatt and Emili groups are now using biochemical procedures to purify and characterize the ~1595 predicted or known membrane-associated protein complexes in S. cerevisiae. With a focus on membrane proteins, we are addressing a significant gap in current databases: ~30% of eukaryotic genomics encode membrane proteins and they account for 50% of drug targets, but structural and functional information about membrane proteins remains relatively sparse. Additionally, we are characterizing the function of ~1000 uncharacterized yeast proteins by determining their structure and catalytic activity, using NMR spectroscopy, X-ray crystallography and a panel of general assays for protein function (e.g. kinases, methyltransferases, acetyltransferases).
