<?xml version="1.0" encoding="UTF-8"?>
<mods xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns="http://www.loc.gov/mods/v3" version="3.1" xsi:schemaLocation="http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-1.xsd">
  <titleInfo>
    <title>In silico characterization of selected orchids’ glycosaminoglycan-related proteins</title>
  </titleInfo>
  <name type="personal">
    <namePart>Nur Izzatul Shahira Binti Zulkifli</namePart>
    <role>
      <roleTerm authority="marcrelator" type="text">creator</roleTerm>
    </role>
    <role>
      <roleTerm type="text">author.</roleTerm>
    </role>
  </name>
  <typeOfResource manuscript="yes">text</typeOfResource>
  <originInfo>
    <place>
      <placeTerm type="code" authority="marccountry">my</placeTerm>
    </place>
    <dateIssued encoding="marc">2025</dateIssued>
    <copyrightDate encoding="marc">2025</copyrightDate>
    <issuance>monographic</issuance>
  </originInfo>
  <language>
    <languageTerm authority="iso639-2b" type="code">eng</languageTerm>
  </language>
  <physicalDescription>
    <form authority="marcform">electronic</form>
    <extent>xiii, 68 pages : illustrations ;</extent>
  </physicalDescription>
  <abstract>This study are focusing on in silico characterization of selected orchid’s glycosaminoglycan- related proteins in which to identify the catalytic regions of selected  orchids’. The orchids are a complex and extensive flowering plant family classified  scientifically as Orchidaceae. They constitute one of the largest flowering plant families,  with approximately 25,000 species and 100,000 hybrids and cultivars. Orchids are valued  for their intricate, vivid blossoms and are frequently linked with beauty, elegance, and  foreignness. Moreover, glycosaminoglycan or (GAGs) is a long, unbranched  polysaccharides composed of repeating disaccharide units. The selected orchid’s that  been selected is Vanda Tan Chay Yan, Phalaenopsis equestris, Dendrobium nobile,  Dendrobium catenatum and Apostasia shenzhenca. All selected orchids had been chose  to do predicted 3D-protein structure by using homology modelling in which the use of  online software tools such as Pyrx, SWISS-MODEL, Bioedit, CASTp,  SAVEs6.0SERVER, BLASTp, Chimera 1.16 and PyMOL. Three online tools (Verify  3D, Procheck, and ERRAT) are used to analyze the quality of 3D-protein structures. The  most suitable models of proteins are then selected through refinement. The Pyrx  platform's Autodock Vina software was used to dock interactions between protein and ligand and compare them to CASTp's predicted active site pocket analysis. Chimera  software was used to visualize the ligand-binding orientation. All of the online software  tools had been using to generate the potential 3D model of selected orchids, it also used  to Molecular docking will be used to study the binding sites of possible ligands to the 3D  structure of a glycosaminoglycan-related protein from chosen orchids. In this research,  there are three type of ligands that been identify which is keratin sulphate, heparin  sulphate and chondroitin sulphate and the ligands were separated with different colours  to easy identifying of their attachment. Overall, it is a success to generate the predicted  molecular docking.</abstract>
  <targetAudience authority="marctarget">specialized</targetAudience>
  <note type="statement of responsibility">Nur Izzatul Shahira Binti Zulkifli</note>
  <note>Faculty of Industrial Sciences and Technology</note>
  <note>Final Year Report (Bachelor of Applied Science in Industrial Biotechnology) -- Universiti Malaysia Pahang Al-Sultan Abdullah - 2025</note>
  <note>Include bibliographical reference</note>
  <subject authority="lcsh">
    <name type="corporate">
      <namePart>Faculty of Industrial Sciences and Technology</namePart>
    </name>
    <topic>Dissertations</topic>
  </subject>
  <subject authority="lcsh">
    <topic>Universities and colleges</topic>
    <topic>Dissertations</topic>
  </subject>
  <subject authority="lcsh">
    <topic>Final Year Report</topic>
    <topic>Dissertations</topic>
  </subject>
  <identifier type="isbn">THE0010314 (Local)</identifier>
  <identifier type="uri">http://umpir.ump.edu.my/id/eprint/45695</identifier>
  <location>
    <url>http://umpir.ump.edu.my/id/eprint/45695</url>
  </location>
  <recordInfo>
    <recordContentSource authority="marcorg">UMPSA</recordContentSource>
    <recordCreationDate encoding="marc">260126</recordCreationDate>
    <recordChangeDate encoding="iso8601">20260126120353.0</recordChangeDate>
    <languageOfCataloging>
      <languageTerm authority="iso639-2b" type="code">eng</languageTerm>
    </languageOfCataloging>
  </recordInfo>
</mods>
