Collective aspects of protein folding illustrated by a toy model.

@article{Stillinger1995CollectiveAO,
  title={Collective aspects of protein folding illustrated by a toy model.},
  author={Stillinger and Head-Gordon},
  journal={Physical review. E, Statistical physics, plasmas, fluids, and related interdisciplinary topics},
  year={1995},
  volume={52 3},
  pages={2872-2877}
}
A simple toy model for polypeptides serves as a testbed to illuminate some nonlocal, or collective, aspects of protein folding phenomena. The model is two dimensional and has only two amino acids, but involves a continuous range of backbone bend angles. Global potential energy minima and their folding structures have been determined for leading members of two special and contrasting polypeptide sequences, center doped and Fibonacci, named descriptively for their primary structures. The results… CONTINUE READING
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