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    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/2052

    Title: Protein Structural Classes Prediction via Residues Environment Profile
    Authors: KA-LOKNG
    Contributors: Department of Biotechnology and Bioinformatics, Asia University
    Keywords: protein classes, solvent accessible arearesidue environment, protein structural profile
    Date: 2006-10
    Issue Date: 2009-10-13 14:57:43 (UTC+8)
    Publisher: Asia University
    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.
    Relation: Asian Journal of Health and Information Sciences 1(3):332-342
    Appears in Collections:[Asian Journal of Health and Information Sciences] v.1 n.3

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