Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis.

@article{Murzin1994PrinciplesDT,
  title={Principles determining the structure of beta-sheet barrels in proteins. I. A theoretical analysis.},
  author={Alexey G. Murzin and Arthur M. Lesk and Cyrus Chothia},
  journal={Journal of molecular biology},
  year={1994},
  volume={236 5},
  pages={1369-81}
}
The major feature of many proteins is a large beta-sheet that twists and coils to form a closed structure in which the first strand is hydrogen bonded to the last: the beta-sheet barrel. McLachlan classified barrels in terms of two integral parameters: the number of strands in the beta-sheet, n, and the "shear number", S, a measure of the stagger of the strands in the beta-sheet. He showed that the mean radius of a barrel and the extent to which strands are tilted relative to its axis are… CONTINUE READING

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