IR study of cross-strand coupling in a β-hairpin peptide using isotopic labels

@article{Setnika2005IRSO,
  title={IR study of cross-strand coupling in a $\beta$-hairpin peptide using isotopic labels},
  author={Vladim{\'i}r Setni{\vc}ka and Rong Xia Huang and C. L. Thomas and Marcus A. Etienne and Jan Kubelka and Robert P. Hammer and Timothy A. Keiderling},
  journal={Journal of the American Chemical Society},
  year={2005},
  volume={127},
  pages={4992-4993}
}
Model β-hairpin peptides can be used to develop understanding of fundamental elements of β-sheet secondary structure formation and stability. We have studied two 13C-labeled variants of a β-hairpin peptide modified from a design originally proposed by Gellman:  Arg-Tyr-Val-Glu-Val-Aib-Gly-Lys-Lys-Ile-Leu-Gln. (In this peptide, the two italicized residues form a β-turn, while 13C-labels are on the amide CO of Val3, Lys8 in HBG-L and Val3, Ile10 in HBG-S.) Both these peptides are labeled on… Expand
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