Determination of the Active Site of Peptidyl-prolyl Isomerase Enzymes Using Peptide-Based Affinity Cleaving Reagents

点击翻译按钮获取中文摘要

Dr. Schepartz proposes to use a new technique - protein affinity cleavage - to analyze the mechanism of protein folding. The method requires the synthesis of bifunctional molecules which contain a protein-cleaving reagent covalently tethered to a protein-binding ligand. Once the ligand is bound the hydroxyl radical is loosed to allow cleavage in the neighborhood of the active site. Analysis of the sites of peptide cleavage will help elucidate the active site and surround to a resolution of single amino acids. It is claimed to be superior in this regard to other techniques, such as affinity labeling experiments. The results from this study promise to provide evidence for this claim and should give interesting data on the peptidy-prolyl isomerase enzymes which will be studied.