The work proposed will develop UV resonance Raman spectroscopy (UVRS) as an incisive technique to examine protein structure and function. We will apply this technique for fundamental studies of amide, peptide and protein excited states and will search for delocalized electronic transitions similar to our recently discovered peptide charge transfer transitions. We will use a photochemical isomerization switching mechanism to determine the amino acid side chain dependence of the ground state trans yields cis peptide activation barriers. We will develop and utilize static and kinetic nsec-msec UVRS methods to examine the unfolding intermediates of proteins such as myoglobin (Mb) and apoM. We will, characterize the dynamical connectivities between adjacent peptide bonds by selectively initiating trans yields cis isomerization in a thioamide substituted peptide, and then measure the conformational changes at adjacent peptide bonds. We will improve UV Raman instrumentation, to increase its sensitivity.
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