Biothermodynamics. Part B [electronic resource] / edited by Michael L. Johnson, Jo M. Holt and Gary K. Ackers.

Includes bibliographical references and indexes.

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 -- 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 -- 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.

Description based on print version record.

The use of thermodynamics in biological research can be equated to an energy book-keeping system. While the structure and function of a molecule is important, it is equally important to know what drives the energy force. These methods look to answer: What are the sources of energy that drive the function? Which of the pathways are of biological significance? As the base of macromolecular structures continues to expand through powerful techniques of molecular biology, such as X-ray crystal data and spectroscopy methods, the importance of tested and reliable methods for answering these questions will continue to expand as well. This volume presents sophisticated methods for estimating the thermodynamic parameters of specific protein-protein, protein-DNA and small molecule interactions. * Elucidates the relationships between structure and energetics and their applications to molecular design, aiding researchers in the design of medically important molecules * Provides a "must-have" methods volume that keeps MIE buyers and online subscribers up-to-date with the latest research * Offers step-by-step lab instructions, including necessary equipment, from a global research community.