Using evolutionary trees in protein secondary structure prediction and other comparative sequence analyses

J Mol Biol. 1996 Oct 25;263(2):196-208. doi: 10.1006/jmbi.1996.0569.


Previously proposed methods for protein secondary structure prediction from multiple sequence alignments do not efficiently extract the evolutionary information that these alignments contain. The predictions of these methods are less accurate than they could be, because of their failure to consider explicitly the phylogenetic tree that relates aligned protein sequences. As an alternative, we present a hidden Markov model approach to secondary structure prediction that more fully uses the evolutionary information contained in protein sequence alignments. A representative example is presented, and three experiments are performed that illustrate how the appropriate representation of evolutionary relatedness can improve inferences. We explain why similar improvement can be expected in other secondary structure prediction methods and indeed any comparative sequence analysis method.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Evolution, Molecular
  • Models, Theoretical*
  • Molecular Sequence Data
  • Protein Structure, Secondary*
  • Proteins* / chemistry
  • Proteins* / genetics
  • Sequence Analysis*


  • Proteins

Associated data

  • SWISSPROT/P07528
  • SWISSPROT/P07986
  • SWISSPROT/P10474
  • SWISSPROT/P14768
  • SWISSPROT/P40942
  • SWISSPROT/P40943
  • SWISSPROT/P40944