Abstract
A secondary structure prediction algorithm is proposed on the hypothesis that short homologous sequences of amino acids have the same secondary structure tendencies. Comparisons are made with the secondary structure assignments of Kabsch and Sander from X‐ray data [(1983) Biopolymers 22, 2577‐2637] and an empirically determined similarity matrix which assigns a sequence similarity score between any two sequences of 7 residues in length. This similarity matrix differs in many respects from that of the Dayhoff substitution matrix [(1978) in: Atlas of Protein Sequence and Structure, (Dayhoff M.O. ed). vol. 5. suppl. 3, pp. 353‐358, National Biochemical Research Foundation, Washington, DC]. This homologue method had a prediction accuracy of 62.2% over 3 states for 61 proteins and 63.6% for a new set of 7 proteins not in the original data base.
Keywords
Similarity (geometry)Protein secondary structureSequence (biology)Structural similarityAlgorithmMatrix (chemical analysis)Computational biologySet (abstract data type)Protein superfamilyMathematicsComputer scienceBiologyChemistryArtificial intelligenceGeneticsBiochemistryGene
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Publication Info
- Year
- 1986
- Type
- article
- Volume
- 205
- Issue
- 2
- Pages
- 303-308
- Citations
- 302
- Access
- Closed
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Cite This
Jonathan M. Levin,
Barry Robson,
Jean Garnier
(1986).
An algorithm for secondary structure determination in proteins based on sequence similarity.
FEBS Letters
, 205
(2)
, 303-308.
https://doi.org/10.1016/0014-5793(86)80917-6
Identifiers
- DOI
- 10.1016/0014-5793(86)80917-6