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    Title: Protein Structural Classes Prediction via Residues Environment Profile
    Authors: 吳家樂;Ng, Ka-Lok
    Contributors: 生物與醫學資訊學系
    Keywords: protein classes;solvent accessible area;residue environment;protein structural profile.
    Date: 2006
    Issue Date: 2012-11-23 17:14:41 (UTC+8)
    Abstract: "We investigate how residue structural and physicochemical environment information, such as the
    protein secondary structure and residue solvent accessibility could be used for protein structural classes
    (all-alpha, all-beta, alpha/beta and alpha+beta) prediction. The residue environment information is
    described by the residue environment profiles which are derived from a relative small set of 500 protein
    sequences having a sequence identity less than 25%. It was demonstrated that this method is able to
    obtain an accuracy of 49.2% for a 4-type class prediction of monomeric and non-disulphide-bonded
    proteins, given the fact that none of the nonclassified protein sequences has a sequence identity higher
    than 25%. This result is comparable to the amino acid composition method which obtains an accuracy
    of 48% for a set of sequences having sequence similarity of less than 30%. The current approach has
    several advantages: (1) it is a physical approach, (2) there is no adjustable parameter, and (3) it is
    simple and efficient."
    Appears in Collections:[Department of Biomedical informatics  ] Journal Article

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