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Evolutionary computation for the prediction of secondary protein structures

Published: 21 March 2011 Publication History
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  • Abstract

    We have developed an evolutionary computation approach to predict secondary structure motifs using some main amino acid physical-chemical properties. The prediction model will consist of rules that predict both the beginning and the end of the regions corresponding to a secondary structure state conformation (α-helix or β-strand). A study about propensities of each pair of amino acids in capping regions of α-helix and β-strand are also performed with a data set of 12,830 non-homologous and non-redundant protein sequences.

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    cover image ACM Conferences
    SAC '11: Proceedings of the 2011 ACM Symposium on Applied Computing
    March 2011
    1868 pages
    ISBN:9781450301138
    DOI:10.1145/1982185
    Permission to make digital or hard copies of all or part of this work for personal or classroom use is granted without fee provided that copies are not made or distributed for profit or commercial advantage and that copies bear this notice and the full citation on the first page. Copyrights for components of this work owned by others than ACM must be honored. Abstracting with credit is permitted. To copy otherwise, or republish, to post on servers or to redistribute to lists, requires prior specific permission and/or a fee. Request permissions from [email protected]

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    Publication History

    Published: 21 March 2011

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    Author Tags

    1. α-helix
    2. β-sheet
    3. β-strand
    4. evolutionary computation
    5. protein secondary structure prediction

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    SAC'11
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    SAC'11: The 2011 ACM Symposium on Applied Computing
    March 21 - 24, 2011
    TaiChung, Taiwan

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