Energetics of Biological Macromolecules, Part B: Volume 295
The very existence of biological structures and their functional interactions are dictated by energetic relationships. Thus the central theme of this volume is that thermodynamic methods, i.e. techniques that probe the energetics of biological macromolecules, now comprise a powerful and practical family of tools for research in modern biology. The application of thermodynamics and statistical thermodynamics to biochemical and biophysical systems is presented. This volume supplements Methods in Enzymology, Volume 259.
General Description of the Series:
The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with more than 300 volumes (all of them still in print), the series contains much material still relevant today--truly an essential publication for researchers in all fields of life sciences.
- Hardback | 548 pages
- 156 x 228 x 30mm | 961.62g
- 02 Sep 1998
- Elsevier Science Publishing Co Inc
- Academic Press Inc
- San Diego, United States
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Table of contents
N.R. Kallenbach and E.J. Spek, Modified Amino Acids as Probes of Helix Stability.
V.J. LiCata and N.M. Allewell, Measuring Hydration Changes of Proteins in Solution: Applications of Osmotic Stress and Structure-Based Calculations.
S.H. White, W.C. Wimley, A.S. Ladokhin, and K. Hristova, Protein Folding in Membranes: Determining Energetics of Peptide-Bilayer Interactions.
M.L. Doyle and P. Hensley, Tight Ligand Binding Affinities Determined from Thermodynamic Linkage to Temperature by Titration Calorimetry.
I. Luque and E. Freire, Structure-Based Prediction of Binding Affinities and Molecular Design of Peptide Ligands.
A.P. Minton, Molecular Crowding: Analysis of Effects of High Concentrations of Inert Cosolutes on Biochemical Equilibria and Rates in Terms of Volume Exclusion.
J.M. Schwehm and W.E. Stites, Application of Automated Methods for Determination of Protein Conformational Stability.
P. Beroza and D.A. Case, Calculations of Proton Binding Thermodynamics in Proteins.
A.L. Klinger and G.K. Ackers, Analysis of Spectra from Multiwavelength Oxygen Binding Studies of Mixed Metal Hybrid Hemoglobins.
L. Benazzi, R. Russo, M. Ripamonti, and M. Perrella, Study of the Bohr Effect in Hemoglobin Intermediates.
P.W. Chun, Application of Planck-Benzinger Relationships to Biology.
T.A. Morton and D.G. Myszka, Kinetic Analysis of Macromolecular Interactions Using Surface Plasmon Resonance Biosensors.
B.M. Baker and K.P. Murphy, Prediction of Binding Energetics from Structure Using Empirical Parameterization.
M.A. McLean, C. Di Primo, E. Deprez, G. Hui Bon-Hoa, and S.G. Sligar, Photoacoustic Calorimetry of Proteins.
H.F. Fisher and J. Tally, Isoergonic Cooperativity: A Novel Form of Allostery.
L. Indyk and H.F. Fisher, Theoretical Aspects of Isothermal Titration Calorimetry.
V.A. Bloomfield and I. Rouzina, Use of Poisson-Boltzmann Equation to Analyze Ion Binding to DNA.
B. Sclavi, S. Woodson, M. Sullivan, M. Chance, and M. Brenowitz, Following the Folding of RNA with Time-Resolved Synchrotron X-Ray Footprinting.
D.F. Senear, L.T. Perini, and S.A. Gavigan, Analysis of Interactions Between CytR and CRP at CytR-Regulated Promoters.
D. Beckett, Energetic Methods to Study Bifunctional Biotin Operon Repressor.
E.K. Merabet, D.S. Burz, and G.K. Ackers, Thermal Melting Properties of C-Terminal Domain Mutants of Bacteriophage l cI Repressor.
J.T. Mason, Investigation of Phase Transitions in Bilayer Membranes.
T.M. Laue, H.K. Shepard, T.M. Ridgeway, T.P. Moody, and T.J. Wilson, Membrane-Confined Analytical Electrophoresis.
"Each chapter is well written, very concise, yet very informative, and should be interesting reading for investigators at different levels of training... The features include many informative illustrations with very useful, very extensive bibliographies... This would be a worthwhile addition to the library of anyone with interests in energetics of protein folding and protein ligand interaction. Since the editors and contributors are internationally recognized experts, the content is very meaningful."
--DOODY'S Publishing Reviews
Praise for the Series
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