Insufficiently dehydrated hydrogen bonds as determinants of protein interactions.

@article{Fernndez2003InsufficientlyDH,
  title={Insufficiently dehydrated hydrogen bonds as determinants of protein interactions.},
  author={Ariel Fern{\'a}ndez and Harold A. Scheraga},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 1},
  pages={
          113-8
        }
}
The prediction of binding sites and the understanding of interfaces associated with protein complexation remains an open problem in molecular biophysics. This work shows that a crucial factor in predicting and rationalizing protein-protein interfaces can be inferred by assessing the extent of intramolecular desolvation of backbone hydrogen bonds in monomeric structures. Our statistical analysis of native structures shows that, in the majority of soluble proteins, most backbone hydrogen bonds… CONTINUE READING
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Biochemistry (Wiley, New York)

  • A. Fernández, A. Colubri, R. S. Berry
  • J. Chem. Phys
  • 2002

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