Spectroscopic evidence for backbone desolvation of helical peptides by 2,2,2-trifluoroethanol: an isotope-edited FTIR study.

@article{Starzyk2005SpectroscopicEF,
  title={Spectroscopic evidence for backbone desolvation of helical peptides by 2,2,2-trifluoroethanol: an isotope-edited FTIR study.},
  author={Agnieszka Starzyk and Wendy Barber-Armstrong and M. K. Sridharan and Sean M. Decatur},
  journal={Biochemistry},
  year={2005},
  volume={44 1},
  pages={369-76}
}
2,2,2-Trifluoroethanol (TFE) is widely used to induce helix formation in peptides and proteins, but the mechanism behind this effect is still poorly understood. Several recent papers have proposed that TFE acts by selectively desolvating the peptide backbone groups of the helix state. Infrared (IR) spectroscopy of the amide I band of polypeptides can be used to probe both secondary structure and backbone solvation, making this technique well suited for addressing the effect of TFE on… CONTINUE READING
15 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 15 extracted citations

Similar Papers

Loading similar papers…