Amino acid substitution matrices from protein blocks. Henikoff, S. & Henikoff, J. G. Proc Natl Acad Sci U S A, 89(22):10915–10919, 1992.
abstract   bibtex   
Methods for alignment of protein sequences typically measure similarity by using a substitution matrix with scores for all possible exchanges of one amino acid with another. The most widely used matrices are based on the Dayhoff model of evolutionary rates. Using a different approach, we have derived substitution matrices from about 2000 blocks of aligned sequence segments characterizing more than 500 groups of related proteins. This led to marked improvements in alignments and in searches using queries from each of the groups.
@Article{henikoff92amino,
  author    = {S. Henikoff and J. G. Henikoff},
  title     = {Amino acid substitution matrices from protein blocks.},
  journal   = {Proc Natl Acad Sci U S A},
  year      = {1992},
  volume    = {89},
  number    = {22},
  pages     = {10915--10919},
  abstract  = {Methods for alignment of protein sequences typically measure similarity by using a substitution matrix with scores for all possible exchanges of one amino acid with another. The most widely used matrices are based on the Dayhoff model of evolutionary rates. Using a different approach, we have derived substitution matrices from about 2000 blocks of aligned sequence segments characterizing more than 500 groups of related proteins. This led to marked improvements in alignments and in searches using queries from each of the groups.},
  file      = {HenikoffHenikoff_AminoAcidSubstitution_PNAS_1992.pdf:1992/HenikoffHenikoff_AminoAcidSubstitution_PNAS_1992.pdf:PDF},
  keywords  = {Amino Acid Sequence; Animals; Caenorhabditis elegans; Drosophila; Lod Score; Mathematics; Molecular Sequence Data; Probability; Proteins; Sequence Homology, Amino Acid},
  owner     = {maltebrinkmeyer},
  pmid      = {1438297},
  timestamp = {2012.02.07},
}

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