Environment-specific amino acid substitution tables: tertiary templates and prediction of protein folds.

@article{Overington1992EnvironmentspecificAA,
  title={Environment-specific amino acid substitution tables: tertiary templates and prediction of protein folds.},
  author={John P. Overington and Dan Donnelly and Mark S. Johnson and Andrej Sali and Tom L. Blundell},
  journal={Protein science : a publication of the Protein Society},
  year={1992},
  volume={1 2},
  pages={216-26}
}
The local environment of an amino acid in a folded protein determines the acceptability of mutations at that position. In order to characterize and quantify these structural constraints, we have made a comparative analysis of families of homologous proteins. Residues in each structure are classified according to amino acid type, secondary structure, accessibility of the side chain, and existence of hydrogen bonds from the side chains. Analysis of the pattern of observed substitutions as a… CONTINUE READING

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