Theoretical Studies of Protein Folding

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Dr. Scheraga is carrying out a combined experimental and theoretical research program designed to elucidate the energies and mechanism of the folding of a polypeptide chain into the native conformation of a protein, and of the action of the resulting protein (enzyme or hormone) on a substrate or receptor. While current potential functions are sufficiently accurate for several of the applications that he has made, his analysis of these potentials (and also of others in the literature) indicates that it is time for a completely new look at the underlying form ( and parameterization of the potentials); this is the first goal of the proposed work. Secondly, some very successful methods have been developed to surmount the multiple-minima problem for small polypeptides and he will devote his efforts to improving them, and extending them to globular proteins containing of the order of 100 residues. He will test the methods on crambin and bovine pancreatic trypsin inhibitor, and then use them to compute the structure of interferon. He will also treat large assemblies of fibrous proteins, viz. collagen.