Helix formation and folding in an artificial peptide
Document Type
Article
Publication Date
8-1-2002
Abstract
Multicanonical simulations with high statistics of a simple artificial peptide, the 25 residue Ala10-Gly5-Ala10 were performed. It was found that this peptide folds into a specific structure that was determined solely by the intrinsic properties of the molecule. At Thc=483±8 K, a helix-coil transition that was either a weak first-order transition or a strong second-order transition was observed.
Publication Title
Journal of Chemical Physics
Recommended Citation
Alves, N.,
&
Hansmann, U.
(2002).
Helix formation and folding in an artificial peptide.
Journal of Chemical Physics,
117(5), 2337-2343.
http://doi.org/10.1063/1.1489419
Retrieved from: https://digitalcommons.mtu.edu/michigantech-p/8819