Photothermal Studies of Fast Peptide/Protein Folding

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Photothermal Studies of Fast Peptide/Protein Folding Randy W. Larsen, Department of Chemistry, University of South Florida, Tampa, FL 33620 Research Focus: The mechanism through which heterogeneous biopolymers fold into specific catalytically active structures is one of the focal points of molecular biophysics. Knowledge of how such processes occur will not only help to understand the molecular basis for a wide range of diseases but will also lead to the design and synthesis of novel biocatalysts. The proposed project utilizes photothermal techniques to obtain DH and DV profiles for fast secondary structure folding associated with small water soluble peptides and proteins. Specific Aims: The specific aims of this project are tto construct thermodynamic and kinetic profiles of (1) photo-triggered helix/coil transitions in small peptides using photothermal methods, (2) photochemicaly triggered folding in b-sheet and b-turn model peptides, and (3) secondary structure folding in the villin head-piece and leucine zipper (GCN-4) peptides.