ASIA unversity:Item 310904400/2570
English  |  正體中文  |  简体中文  |  全文笔数/总笔数 : 94286/110023 (86%)
造访人次 : 21710086      在线人数 : 485
RC Version 6.0 © Powered By DSPACE, MIT. Enhanced by NTU Library IR team.
搜寻范围 查询小技巧:
  • 您可在西文检索词汇前后加上"双引号",以获取较精准的检索结果
  • 若欲以作者姓名搜寻,建议至进阶搜寻限定作者字段,可获得较完整数据
  • 进阶搜寻


    jsp.display-item.identifier=請使用永久網址來引用或連結此文件: http://asiair.asia.edu.tw/ir/handle/310904400/2570


    题名: PDST:Protein Drug Stability Tuner a web server to improve the stability of protein drug
    作者: Yueh-Feng Wu
    贡献者: Department of Bioinformatics
    关键词: Protein Drug;stability;Thermodynamic
    日期: 2006
    上传时间: 2009-11-06 14:32:06 (UTC+0)
    出版者: Asia University
    摘要: The drug stability include half life and ADME are the important factors that influence the drug efficacy. However, the resource of a number of drugs are come from proteins or peptides, which can be modified and reconstituted for every purpose. How to increase protein drug stability is the main challenge for pharmaceutical study.
    There are many ways to solve the problem. For example, we can enhance ionic pair, hydrophobic interaction, and hydrogen bond etc. Our tool provides prediction and modification for protein stability by calculate Temperature Index (TI) and Instability Index (II). The Temperature Index (TI) was applied to determine the Tm (Melting Temperature) directly from protein sequences.
    PDST(Protein Drug Stability Tuner) is a novel web online tool to provide analyzing protein drug stability and suggesting the mutation by inputting primary sequences of proteins. PDST is a freely available at http://biotuner.bio.ncue.edu.tw/pdst.htm We integrate PDB and Drug Bank, these two databases calculate the TI and II of these proteins, test and verify the result of analyzing. In according to the result, we build up a new database to provide the query of stability of protein drug.
    显示于类别:[生物資訊與醫學工程學系 ] 博碩士論文

    文件中的档案:

    档案 大小格式浏览次数
    0KbUnknown526检视/开启


    在ASIAIR中所有的数据项都受到原著作权保护.


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