English  |  正體中文  |  简体中文  |  Items with full text/Total items : 90074/105197 (86%)
Visitors : 7156452      Online Users : 34
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
Scope Tips:
  • please add "double quotation mark" for query phrases to get precise results
  • please goto advance search for comprehansive author search
  • Adv. Search
    HomeLoginUploadHelpAboutAdminister Goto mobile version

    Please use this identifier to cite or link to this item: http://asiair.asia.edu.tw/ir/handle/310904400/2542

    Title: Analysis of protein secondary structures and residues environment
    Authors: Kuo-Ching, Hsiao
    Contributors: Department of Bioinformatics
    Keywords: protein structures;environment score matrix;structure profiles;sequence and structure alignment;protein classes classification prediction
    Date: 2005
    Issue Date: 2009-11-06 22:31:39 (UTC+8)
    Publisher: Asia University
    Abstract: In this thesis, I investigated how the amino acids physicochemical environment information, such as the protein secondary structures and residues solvent accessibility, could possibly enhance one’s capability for protein classes classification prediction.
    The score matrices for several classes (all-, all-,  and according to the SCOP classification) of known protein sequences were computed. Sequences are taken from a protein secondary structure database, for example, the DSSP secondary structure protein databases. Thus, one can construct the 3D structure profiles for each entry in the PDB database. These profiles are used to score the query protein sequence to be modeled for compatibility with the known classes classification.
    To demonstrate the 3D structure profile method is able to detect sequences compatible with a known class, one aligns the query sequences with the environment of a known protein structure using a simple sequence alignment algorithm. My study indicated that the method has larger than 95% accuracy in protein classes assignment(average score <0.5). Furthermore, I had also established the fact that the structure profile approach is able to detect distant sequences well below the twilight zone (less than 25% sequence similarity).
    Appears in Collections:[生物資訊與醫學工程學系 ] 博碩士論文

    Files in This Item:

    File SizeFormat

    All items in ASIAIR are protected by copyright, with all rights reserved.

    DSpace Software Copyright © 2002-2004  MIT &  Hewlett-Packard  /   Enhanced by   NTU Library IR team Copyright ©   - Feedback