Contributions of residue pairing to beta-sheet formation: conservation and covariation of amino acid residue pairs on antiparallel beta-strands.

@article{MandelGutfreund2001ContributionsOR,
  title={Contributions of residue pairing to beta-sheet formation: conservation and covariation of amino acid residue pairs on antiparallel beta-strands.},
  author={Yael Mandel-Gutfreund and S. K. Zaremba and L. M. Gregoret},
  journal={Journal of molecular biology},
  year={2001},
  volume={305 5},
  pages={1145-59}
}
In an effort to better understand beta-sheet assembly, we have investigated the evolutionary behavior of neighboring residues on adjacent antiparallel beta-strands. Residue pairs were classified according to solvent exposure as well as by whether their backbone NH and C==O groups are hydrogen bonded. The conservation and covariation of 19,241 pairs in 219 sequence alignments was analyzed. Buried pairs were found to be the most conserved, while stronger covariation was detected in the solvent… CONTINUE READING

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The interpretation of protein structures: total volume, group volume distributions and packing density

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