Conformations and free energy landscapes of polyproline peptides.

  title={Conformations and free energy landscapes of polyproline peptides.},
  author={Mahmoud Moradi and Volodymyr Babin and Christopher Roland and Thomas A. Darden and Celeste Sagui},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  volume={106 49},
The structure of the proline amino acid allows folded polyproline peptides to exist as both left- (PPII) and right-handed (PPI) helices. We have characterized the free energy landscapes of hexamer, nanomer, and tridecamer polyproline peptides in gas phase and implicit water as well as explicit hexane and 1-propanol for the nanomer. To enhance the sampling provided by regular molecular dynamics, we used the recently developed adaptively biased molecular dynamics method, which describes Landau… CONTINUE READING


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