Cis-trans proline isomerization effects on collagen triple-helix stability are limited.

@article{Dai2009CistransPI,
  title={Cis-trans proline isomerization effects on collagen triple-helix stability are limited.},
  author={Nan Dai and Felicia A. Etzkorn},
  journal={Journal of the American Chemical Society},
  year={2009},
  volume={131 38},
  pages={13728-32}
}
We investigated the effect of restricting cis-trans proline isomerization on collagen triple-helix stability. The Pro residues at the Xaa and Yaa positions of an (Xaa-Yaa-Gly) triplet were replaced by a Pro-trans-Pro alkene isostere in the host-guest peptide, H-(Pro-Pro-Gly)(10)-OH. The resulting alkene isostere peptide had a T(m) value 53.6 degrees C lower than that of the control peptide. The Pro-trans-Pro alkene isostere peptide had a T(m) value 3.9 degrees C higher than that of the… CONTINUE READING
10 Citations
0 References
Similar Papers

Similar Papers

Loading similar papers…