The Resource Biothermodynamics, edited by Michael L. Johnson, Jo M. Holt, Gary K. Ackers, (electronic resource)

Biothermodynamics, edited by Michael L. Johnson, Jo M. Holt, Gary K. Ackers, (electronic resource)

Statement of responsibility
edited by Michael L. Johnson, Jo M. Holt, Gary K. Ackers
Member of
Cataloging source
Dewey number
  • illustrations
  • plates
index present
LC call number
  • QP601
  • QP601
LC item number
  • .C71
  • .M49 vol. 455
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
Series statement
Methods in enzymology,
Series volume
v. 455, 466
Biothermodynamics, edited by Michael L. Johnson, Jo M. Holt, Gary K. Ackers, (electronic resource)
Bibliography note
Includes bibliographical references and indexes
  • net
black and white
  • Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models
  • Tural Aksel, Doug Barrick
  • Isothermal titration calorimetry : general formalism using binding polynomials
  • Ernesto Freire, Arne Schön, Adrian Velazquez-Campoy
  • Kinetic and equilibrium analysis of the myosin ATPase
  • Enrique M. De La Cruz, E. Michael Ostap
  • The Hill coefficient : inadequate resolution of cooperativity in human hemoglobin
  • Jo M. Holt, Gary K. Ackers
  • Methods for measuring the thermodynamic stability of membrane proteins
  • Heedeok Hong ... [et al.]
  • pt. A. (v. 455)
  • NMR analysis of dynein light chain dimerization and interactions with diverse ligands
  • Gregory Benison, Elisar Barbar
  • Characterization of parvalbumin and polcalcin divalent ion binding by isothermal titration calorimetry
  • Michael T. Henzl
  • Energetic profiling of protein folds
  • Jason Vertrees, James O. Wrabl, Vincent J. Hilser
  • Model membrane thermodynamics and lateral distribution of cholesterol : from experimental data to Monte Carlo simulation
  • Juyang Huang
  • Thinking inside the box : designing, implementing, and interpreting thermodynamic cycles to dissect cooperativity in RNA and DNA folding
  • Nathan A. Siegfried, Philip C. Bevilacqua
  • Biothermodynamics.
  • The thermodynamics of virus capsid assembly
  • Sarah Katen, Adam Zlotnick
  • Extracting equilibrium constants from kinetically limited reacting systems
  • John J. Correia, Walter F. Stafford
  • Practical approaches to protein folding and assembly : spectroscopic strategies in thermodynamics and kinetics
  • Jad Walters, Sara L. Milam, A. Clay Clark
  • Using thermodynamics to understand progesterone receptor function : method and theory
  • Keith D. Connaghan-Jones, David L. Bain
  • Direct quantitation of Mg(superscript 2+)-RNA interactions by use of a fluorescent dye
  • Dan Grilley, Ana Maria Soto, David E. Draper
  • Examining cooperative gating phenomena in voltage-dependent potassium channels: taking the energetic approach
  • Thermal stability of collagen triple helix
  • Electrostatic contributions to the stabilities of native proteins and amyloid complexes
  • Kinetics of allosteric activation
  • Thermodynamics of the protein translocation
  • Thermodynamic analysis of the structure-function relationship in the total DNA-binding site of enzyme-DNA complexes
  • Equilibrium and kinetic approaches for studying oligomeric protein folding
  • Methods for quantifying T cell receptor binding affinities and thermodynamics
  • Thermodynamic and kinetic analysis of bromodomain-histone Interactions
  • Thermodynamics of 2-Cys Peroxiredoxin assembly determined by isothermal titration calorimetry
  • pt. B (v. 466).
  • Protein-lipid interactions: Role of membrane plasticity and lipid specificity on peripheral protein interactions
  • Predicting pKa values with continuous constant pH molecular dynamics
  • Unfolding thermodynamics of DNA intramolecular complexes Involving joined triple- and double-helical motifs
  • Thermodynamics and conformational change governing domain-domain interactions of calmodulin
  • Use of pressure perturbation calorimetry to characterize the volumetric properties of proteins
  • Solvent denaturation of proteins and interpretations of the M value
  • Measuring cotranslational folding of nascent polypeptide chains on ribosomes
  • Using NMR-detected backbone amide 1H exchange to assess macromolecular crowding effects on globular-protein stability
  • Fluorescence spectroscopy in thermodynamic and kinetic analysis of pH-dependent membrane protein Insertion
  • Evaluating the energy-dependent "binding"in the early stage of protein import into chloroplasts
  • Use of DNA length variation to detect periodicities in positively cooperative, nonspecific binding
  • The impact of ions on allosteric functions in human liver pyruvate kinase
  • Conformational stability of cytochrome c probed by optical spectroscopy
  • Examining ion channel properties using free-energy methods
Control code
1 online resource
Form of item
Other physical details
ill. (some col.)
Specific material designation
System control number
  • (OCoLC)465215456
  • sciencedirect0123745969

Library Locations

    • Deakin University Library - Geelong Waurn Ponds CampusBorrow it
      75 Pigdons Road, Waurn Ponds, Victoria, 3216, AU
      -38.195656 144.304955
Processing Feedback ...