Incorporation of non-local interactions in protein secondary structure prediction from the amino acid sequence.
Existing approaches to protein secondary structure prediction from the amino acid sequence usually rely on the statistics of local residue interactions within a sliding window and the secondary structural state of the central residue. The practically achieved accuracy limit of such single residue and single sequence prediction methods is 65% in three structural stages (alpha-helix, beta-strand and coil). Further improvement in the prediction quality is likely to require exploitation of various aspects of three-dimensional protein architecture. Here we make such an attempt and present an accurate algorithm for secondary structure prediction based on recognition of potentially hydrogen-bonded residues in a single amino acid sequence. The unique feature of our approach involves database-derived statistics on residue type occurrences in different classes of beta-bridges to delineate interacting beta-strands. The alpha-helical structures are also recognized on the basis of amino acid occurrences in hydrogen-bonded pairs (i,i + 4). The algorithm has a prediction accuracy of 68% in three structural stages, relies only on a single protein sequence as input and has the potential to be improved by 5-7% if homologous aligned sequences are also considered.
Frishman
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D
European Molecular Biology Laboratory, Heidelberg, Germany.
Argos
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P
D000465:Algorithms; D000595:Amino Acid Sequence; D003195:Computer Communication Networks; D006860:Hydrogen Bonding; D007256:Information Systems; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D012984:Software