The major goal of this project is to obtain sufficient data on the thermodynamic stability of peptide secondary structure models to develop and implement an algorithm for predicting the local structuring propensities of polypeptides purely based on the primary structure, the amino acid sequence of both peptides and natural proteins. Specifically, the thermodynamic and kinetic consequences of helix N- and C-capping and the intrinsic helical propensities of different residues will be determined. In addition, designed beta-hairpins and beta-sheets will be studied to determine the cooperativity of beta-structure formation, and the relative contributions of turn propensity and cross-strand hydrophobic interactions to the thermodynamic stability of beta-systems.
With this award, the Organic and Macromolecular Chemistry Program is supporting the research of Professor Niels H. Andersen, of the Department of Chemistry at University of Washington. Professor Andersen's research efforts focus on the understanding of peptide secondary structure, which is essential for a complete understanding of protein folding. Such studies will be useful for designing artificial systems with protein-like functional properties and for re-engineering natural systems. They could also lead to a better understanding of amyloid diseases and the development of peptide based drugs.
