We will continue developing UV resonance Raman spectroscopy ('UVRS) as an incisive technique for examining amide excited states, and biomolecular structure and function. We will measure UVRS excitation profiles of peptides and proteins to examine the excited states of the different secondary structure motifs. These studies will also characterize the solution conformational distributions of small peptides. We will develop UVRS methodologies to monitor hydrophobic collapse and ordering of hydrophobic domains. The results above will be utilized in a detailed study of the first stages of peptide folding and unfolding between a-helix and random coil structures, and between fl-sheet and random coil structures. We will experimentally probe the kinetics of protein folding to differentiate between the different dynamics hypothesized by the framework model compared to the hydrophobic collapse mode. We will continue to advance the enabling UV Raman instrumentation with the objective of increasing sensitivity, selectivity and information content.
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