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:
    non sort: The
    title: X-ray crystal structure of bovine (gamma symbol)-carboxypeptidase A
  name:
    name part: Melton, Tammy Janine
    name part: 1960-
    role:
      role term: creator
  name:
    name part: Cotton, F. Albert
    role:
      role term: degree supervisor.
  name:
    name part: Hall, Michael B.
    role:
      role term: degree committee member.
  name:
    name part: Hazen, Edward E.
    role:
      role term: degree committee member.
  name:
    name part: Melton, James R.
    role:
      role term: degree committee member.
  name:
    name part: Texas A & M University
    role:
      role term: degree granting institution.
  type of resource: text
  genre: bibliography
  genre: Academic theses
  origin info:
    place:
      place term: xx
    date issued: 1986
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: print
    extent: xii, 134 leaves : illustrations ; 29 cm
  abstract: The structure of [gamma]-carboxypeptidase A from bovine pancreas has been determined by single-crystal X-ray crystallography at 2.0 [angstrom] with a final Residual R factor of 0.250. Multiple isomorphous replacement, an entropy-maximization procedure, and least squares refinement were used to determine the structure. The molecule has a zinc atom at the active site which is coordinated to His 69, His 196, and Glu 72. The enzyme crystallizes in space group P2[1] with unit cell parameters: a = 51.35(3) [angstrom], b = 57.77(2) [angstrom], c = 45.33(3) [angstrom], β = 94.85(6)°, V = 133,990 [angstrom]^3. There are two molecules per unit cell. The structure of CPA[gamma] is more diffuse than CPA[α]; it is approximately 15 to 20% larger. The hydrogen bonding which is present within the molecule is weaker, mostly as a result of the nearby segments of polypeptide backbone having been spread farther apart. Three cis-peptides are present in CPA[gamma] and occur between Ser 197 and Tyr 198, Pro 205 and Tyr 206, and Arg 272 and Asp 273. All these are immediately adjacent to catalytically important residues. The Tyr 248 -OH group is in the "up" position as would be expected for a non-substrate-bound structure (free enzyme.) Its distance from the active site appears greater than could be overcome by simple movements of the polypeptide backbone. Glu 270 appears near the active site. The carboxylate oxygens are 4.6 and 4.2 [angstrom] away from zinc. The elements of primary, secondary, and tertiary structure are presented and discussed. A list of refined atomic parameters is presented in Appendix B.
  note: "Major subject: Chemistry."
  note: Typescript (photocopy).
  note: Vita.
  note: Ph. D. Texas A & M University 1986
  note: Includes bibliographical references (leaves 78-80).
  subject:
    topic: Carboxypeptidases
  subject:
    topic: Enzymatic analysis
  subject:
    topic: X-ray crystallography
  subject:
    topic: Major chemistry
  identifier: http://proxy.library.tamu.edu/login
  identifier: https://hdl.handle.net/1969.1/DISSERTATIONS-24844
  related item:
    location:
      url: http://proxy.library.tamu.edu/login
  related item:
    location:
      url: https://hdl.handle.net/1969.1/DISSERTATIONS-24844
  record info:
    record content source: TXA
    record creation date: 880620
    record change date: 20220104090745.0
    record identifier: in00000016874
    language of cataloging:
      language term: eng