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: Energetics of biological macromolecules
    part number: Part D
  name:
    name part: Holt, Jo M.
  name:
    name part: Johnson, Michael L.
    name part: 1947-
  name:
    name part: Ackers, Gary K.
  type of resource: text
  genre: bibliography
  genre: Electronic books.
  origin info:
    place:
      place term: ne
    place:
      place term: Amsterdam
    place:
      place term: Boston
    publisher: Elsevier/Academic Press
    date issued: ©2004
    date issued: 2004
    issuance: monographic
  language:
    language term: eng
  physical description:
    form: remote
    extent: 1 online resource (xxxii, 281 pages, [4] pages of plates) : illustrations (some color).
  abstract: This volume focuses on the cooperative binding aspects of energetics in biological macromolecules. Methodologies such as NMR, small-angle scattering techniques for analysis, calorimetric analysis, fluorescence quenching, and time resolved FRET measurements are discussed.
  table of contents: 1. Analyzing intermediate state cooperativity in hemoglobin -- 2. Nuclear magnetic resonance spectroscopy in the study of hemoglobin cooperativity -- 3. Evaluating cooperativity in dimeric hemoglobins -- 4. Measuring assembly and binding in human embryonic hemoglobins -- 5. Small-angle scattering techniques for analyzing conformational transitions in hemocyanins -- 6. Multivalent protein-carbohydrate interactions: isothermal titration microcalorimetry studies -- 7. Calorimetric analysis of mutagenic effects on protein-ligand interactions -- 8. Multiple binding of ligands to a linear biopolymer -- 9. Probing site-specific energetics in proteins and nucleic acids by hydrogen exchange and nuclear magnetic resonance spectroscopy -- 10. Fluorescence quenching methods to study protein-nucleic acid interactions -- 11. Thermodynamics, protein modification, and molecular dynamics in characterizing lactose repressor protein: strategies for complex analyses of protein structure-function -- 12. Linked equilibria in biotin repressor function: thermodynamic, structural and kinetic analysis -- 13. Distance parameters derived from time-resolved Forster resonance energy transfer measurements and their use in structural interpretations of thermodynamic quantities associated with protein-DNA interactions.
  note: edited by Jo M. Holt, Michael L. Johnson, Gary K. Ackers.
  note: Includes bibliographical references and indexes.
  subject:
    topic: Macromolecules
  subject:
    topic: Bioenergetics
  subject:
    topic: Cooperative binding (Biochemistry)
  subject:
    topic: Allosteric proteins
  subject:
    topic: Thermodynamics
  subject:
    topic: SCIENCE
    topic: Life Sciences
    topic: Biochemistry
  subject:
    topic: Allosteric proteins
  subject:
    topic: Bioenergetics
  subject:
    topic: Cooperative binding (Biochemistry)
  subject:
    topic: Macromolecules
  subject:
    topic: Thermodynamics
  subject:
    topic: Macromolecular Substances [MESH]
  subject:
    topic: Enzymes [MESH]
  subject:
    topic: Protein Folding [MESH]
  classification: QP601 .M49eb vol. 379
  classification: 572/.7
  classification: QU135 MET
  related item:
    title info:
      title: Energetics of biological macromolecules. Part D
    origin info:
      publisher: Amsterdam ; Boston : Elsevier/Academic Press, ©2004
    identifier: (OCoLC)54685200
  related item:
    title info:
      title: Methods in enzymology ; v. 379
  identifier: 9780080497174
  identifier: 0080497179
  identifier: 0121827836
  identifier: 9780121827830
  identifier: 1281011460
  identifier: 9781281011466
  identifier: https://www.sciencedirect.com/science/bookseries/00766879/379
  record info:
    record content source: N$T
    record creation date: 070823
    record change date: 20180501121913.0
    record identifier: ocn166274283
    language of cataloging:
      language term: eng