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: Isoelectric trapping and mass spectrometry
    sub title: tools for proteomics
  name:
    name part: Cologna, Stephanie Marie.
    role:
      role term: creator
  name:
    name part: Russell, David H.
    role:
      role term: thesis advisor.
  type of resource: text
  genre: bibliography
  origin info:
    place:
      place term: txu
    date issued: 2012
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: remote
    extent: 1 online resource.
  abstract: Mass spectrometry (MS) has played a major role in the proteomic analysis of an array of biological samples. Even so, inherent limitations exist such as sample complexity and the dynamic range. In an attempt to overcome these limitations, prefractionation is typically performed followed by reversed phase liquid chromatography coupled with MS. Pre-fractionation can be performed in several formats including chromatographic or electrophoretic based methods. Solution-based isoelectric point (pI) fractionation, specifically isoelectric trapping (IET), provides an attractive alternative for pre-fractionation in bottom-up proteomic studies. A recently developed device, membrane separated wells for isoelectric focusing and trapping (MSWIFT), provides rapid separation on the basis of pI and resulting solutions are MS compatible without the need for extensive sample cleanup. Initial experiments demonstrate fractionation using MSWIFT, of peptide mixtures ranging from standards to a yeast lysate where resulting fractions are analyzed using matrixassisted laser desorption/ionization (MALDI) -- MS or further separated using reversed phase liquid chromatography followed by tandem MS (MS/MS) analysis. Identified yeast proteins range in size, pI and copy number illustrating an ability to increase the depth of proteome coverage when using MSWIFT. Extensive studies were also performed using MSWIFT in a multi-stage fractionation platform to improve peptide and protein identifications for the first large-scale proteomic study of the model fungus, Neurospora crassa. A second focus of this work is the development of a new sample preparation method for proteolytic digestion and high-throughput separations using MSWIFT. Histidine is used as a neutral pH, isoelectric, sample buffer for tryptic digestion of proteins and also assists in rapid separations using MSWIFT owing to the low conductivity. Tryptic digests of individual standard proteins and a mixture of standard proteins are used to ill…
  note: by Stephanie Marie Cologna.
  note: "Major Subject: Chemistry"
  note: Electronic resource.
  note: Doctor of Philosophy Texas A&M University 2010 http://hdl.handle.net/1969.1/ETD-TAMU-2010-12-8593
  note: Includes bibliographical references.
  note: Text (Dissertation)
  subject:
    topic: Major chemistry
  subject:
    topic: MALDI
  subject:
    topic: IEF
  subject:
    topic: pI
  subject:
    topic: MS
  subject:
    topic: Isoelectric Point
  subject:
    topic: ESI
  subject:
    topic: Mass Spectrometry
  subject:
    topic: IET
  identifier: http://hdl.handle.net/1969.1/ETD-TAMU-2010-12-8593
  record info:
    record content source: TXA
    record creation date: 120313
    record change date: 20151202151735.0
    record identifier: in00002737788