@article{pittir17246,
          volume = {49},
          number = {15},
           month = {April},
          author = {K Xiong and SA Asher},
           title = {Circular dichroism and UV resonance raman study of the impact of alcohols on the gibbs free energy landscape of an {\ensuremath{\alpha}}-helical peptide},
         journal = {Biochemistry},
           pages = {3336 -- 3342},
            year = {2010},
             url = {http://d-scholarship-dev.library.pitt.edu/17246/},
        abstract = {We used CD and UV resonance Raman spectroscopy to study the impact of alcohols on the conformational equilibria and relative Gibbs free energy landscapes along the Ramachandran {\ensuremath{\phi}}-coordinate of a mainly poly-Ala peptide, AP with an AAAAA(AAARA)3A sequence. 2,2,2-Trifluoroethanol (TFE) most stabilizes the {\ensuremath{\alpha}}-helix-like conformations, followed by ethanol, methanol, and pure water. The {\ensuremath{\pi}}-bulge conformation is stabilized more than the {\ensuremath{\alpha}}-helix, while the 310-helix is destabilized due to the alcohol-increased hydrophobicity. Turns are also stabilized by alcohols. We also found that while TFE induces more {\ensuremath{\alpha}}-helices, it favors multiple, shorter helix segments. {\copyright} 2010 American Chemical Society.}
}