Helix formation and folding in an artificial peptide
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.
Journal of Chemical Physics
Helix formation and folding in an artificial peptide.
Journal of Chemical Physics,
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