@article{pittir17234,
          volume = {2},
          number = {4},
           month = {February},
          author = {SA Oladepo and K Xiong and Z Hong and SA Asher},
           title = {Elucidating peptide and protein structure and dynamics: UV resonance raman spectroscopy},
         journal = {Journal of Physical Chemistry Letters},
           pages = {334 -- 344},
            year = {2011},
             url = {http://d-scholarship-dev.library.pitt.edu/17234/},
        abstract = {UV resonance Raman spectroscopy (UVRR) is a powerful method that has the requisite selectivity and sensitivity to incisively monitor biomolecular structure and dynamics in solution. In this Perspective, we highlight applications of UVRR for studying peptide and protein structure and the dynamics of protein and peptide folding. UVRR spectral monitors of protein secondary structure, such as the amide III3 band and the C{\ensuremath{\alpha}}-H band frequencies and intensities, can be used to determine Ramachandran {\ensuremath{\psi}} angle distributions for peptide bonds. These incisive, quantitative glimpses into conformation can be combined with kinetic T-jump methodologies to monitor the dynamics of biomolecular conformational transitions. The resulting UVRR structural insight is impressive in that it allows differentiation of, for example, different {\ensuremath{\alpha}}-helix-like states that enable differentiating {\ensuremath{\pi}} and 310 states from pure {\ensuremath{\alpha}}-helices. These approaches can be used to determine the Gibbs free-energy landscape of individual peptide bonds along the most important protein (un)folding coordinate. Future work will find spectral monitors that probe peptide bond activation barriers that control protein (un)folding mechanisms. In addition, UVRR studies of side chain vibrations will probe the role of side chains in determining protein secondary, tertiary, and quaternary structures. {\copyright} 2011 American Chemical Society.}
}