Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone.

@article{Stites1995EmpiricalEO,
  title={Empirical evaluation of the influence of side chains on the conformational entropy of the polypeptide backbone.},
  author={Wesley E. Stites and Julianto Pranata},
  journal={Proteins},
  year={1995},
  volume={22 2},
  pages={132-40}
}
Changes in amino acid side chains have long been recognized to alter the range and distribution of phi, psi angles found in the main chain of polypeptides. Altering the range and distribution of phi, psi angles also alters the conformational entropy of the flexible denatured state and may thus stabilize or destabilize it relative to the comparatively conformationally rigid native state. A database of 12,320 residues from 61 nonhomologous, high resolution crystal structures was examined to… CONTINUE READING

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