rdf-syntax-grammar
mods:
  schema location: http://www.loc.gov/mods/v3 http://www.loc.gov/standards/mods/v3/mods-3-2.xsd
  title info:
    title: Structural Study of Lipid-binding Proteins
  name:
    name part: Tsai, Han-Chun
    role:
      role term: creator
    role:
      role term: author.
  name:
    name part: Sacchettini, James C.
    role:
      role term: thesis advisor.
  name:
    name part: Texas A & M University
    role:
      role term: degree granting institution.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2013
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: remote
    extent: 1 online resource.
  abstract: Tuberculosis and malaria are among the most deadly infectious diseases in the world. The prevalence in regions without well-established public health causes economical and financial burdens for both society and patients. There is an urgent need to find effective treatments due to the emergence of drug-resistant strains. The aim of the studies reported here was to gain knowledge from the protein structures that can lead to the elimination of these pathogens. In these studies, protein crystallography is the main method used to solve protein structure. Based on the protein structure, we used different methods to characterize the protein function of three lipid-binding proteins (LprG, LprA, and gp232), and to identify potent inhibitors against Plasmodium falciparum enoyl-ACP reductase (PfENR), a drug target protein involved in central lipid metabolism. To characterize the function of two lipid-binding proteins (LprG and LprA), liquid chromatography-mass spectrometry (LC-MS) was used to analyze the ligand extract. In the study of tail fiber protein from mycobacteriophage, we used protein sequence alignment to identify gp232 as a major tail fiber protein, which potentially binds to lipids on the cellular surface of mycobacteria. A pull-down assay and imaging methods (fluorescence microscopy and electron microscopy) were conducted to confirm the function of gp232. In the structural study of PfENR, the structure-activity relationships method was used to find potent inhibitors against PfENR, which would show stronger inhibition than the known inhibitor triclosan. The triclosan-like analogs with modification at the 5-position revealed a new binding site in PfENR that has great potential for improving the potency of inhibition. We found that two inhibitors containing the core structure of piperidine and tetrahydroquinoline reached this new binding site and were 10-fold more potent than triclosan. The structural study of PfENR provides structural insights into the inhibitor-bin…
  note: by Han-Chun Tsai.
  note: "Major Subject: Chemistry"
  note: Includes vita.
  note: Doctor of Philosophy Texas A & M University 2013 http://hdl.handle.net/1969.1/151067
  note: Includes bibliographical references.
  note: Text (Dissertation)
  subject:
    topic: Major Chemistry
  subject:
    topic: Mycobacterium tuberculosis
  subject:
    topic: protein structure
  subject:
    topic: lipoprotein
  subject:
    topic: PfENR
  subject:
    topic: mycobacteriophage
  subject:
    topic: tail fiber protein
  identifier: http://hdl.handle.net/1969.1/151067
  record info:
    record content source: TXA
    record creation date: 140227
    record change date: 20151206092157.0
    record identifier: in00003478237
    language of cataloging:
      language term: eng