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An algorithm for secondary structure determination in proteins based on sequence similarity

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Levin, Jonathan M., Robson, Barry, Garnier, Jean·1986·FEBS Letters

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.

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Metadata

Authors
Levin, J. M., Robson, B., & Garnier, J.
Venue
FEBS Letters
Publisher
Wiley
Published
1986-09-15
Volume
205
Issue
2
Pages
303-308
ISSN
  • 0014-5793 (ISSN-L)
  • 1873-3468
OpenAlex
W2073739993
Cited by
301
References
1
FWCI
4.14
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: An algorithm for secondary structure determination in proteins based on sequence similarity. https://app.cochat.ai/papers/10.1016/0014-5793(86)80917-6
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Levin, J. M., Robson, B., & Garnier, J. (1986). An algorithm for secondary structure determination in proteins based on sequence similarity. FEBS Letters. https://doi.org/10.1016/0014-5793(86)80917-6

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

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