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: Cation Binding and the Conformational Stability of Ribonuclease T1
  name:
    name part: Erickson, Rick.
    role:
      role term: creator
  name:
    name part: Pace, C. N.
    role:
      role term: degree supervisor.
  type of resource: software, multimedia
  genre: Undergraduate thesis
  origin info:
    place:
      place term: txu
    date issued: 1990
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: electronic
    extent: 1 online resource (29 pages).
  abstract: The Asp15-->Ala mutant of ribonuclease T1 (RNase T1) was constructed by site-directed mutagenesis, cloned and expressed in Escherichia coli. This mutant was synthesized to determine whether or not the aspartic acid at position 15 is a cation binding site as predicted by x-ray crystallography. The conformational stability of the mutant's folded state increased by 0.97 kcal/mol in 0.15M NaCl and by 1.33 kcal/mol in 0.20M CaCl2. These results indicate that cations are still being bound by the mutant. This means that our previous thoughts on the contribution of the cation binding site to the stability of RNase T1 were not correct and that further studies are needed.
  target audience: specialized
  note: Undergraduate thesis written for Program year: 1989/1990
  note: Digitized from print version held at Pickle Center High Density Storage, barcode 24829692
  note: University Undergraduate Fellow, sponsored by Biochemistry Department.
  note: HDR
  subject:
    topic: cation binding site
  subject:
    topic: cations
  subject:
    topic: Escherichia coli
  subject:
    topic: stability
  identifier: https://oaktrust.library.tamu.edu/handle/1969.1/CAPSTONE-EricksonR_1990
  record info:
    record creation date: 231116
    record change date: 20240301201130.5
    record identifier: in00004780636