Energetics of Biological Macromolecules

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ISBN: 9780121821609 | 0121821609
Cover: Hardcover
Copyright: 9/25/1995

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This volume focuses on methods related to allosteric enzymes and receptors, including fluorescent proves, spectroscopic methods and quantitative analysis as well as on cooperativity in protein folding. NMR and mass spectrometry methods are discussed.*Allosteric Enzymes and Receptors*Cooperativity in Protein Folding and Assembly

Pathway of Allosteric Control as Revealed by Intermediate States of Hemoglobin
Probes of Energy Transduction in Enzyme Catalysis
Macromolecules and Water: Probing with Osmotic Stress
Linkage of Protein Assembly to Protein-DNA Binding
Linkage at Steady State: Allosteric Transitions of Thrombin
Thermal Denaturation Methods in Study of Protein Folding
Kinetics of Lipid Membrane Phase Transitions: A Volume Perturbation Calorimeter Study
Tight Binding Affinities Determined from the Thermodynamic Linkage to Protons by Titration Calorimetry
Calorimetric Methods for Interpreting Protein-Ligand Interactions
Extracting Thermodynamic Data from Equilibrium Melting Curves for Oligonucleotide Order-Disorder Transitions
Predicting Thermodynamic Properties of RNA
Thermodynamics and Mutations in RNA-Protein Interactions
Melting Studies of RNA Unfolding and RNA-Ligand Interactions
Structural-Perturbation Approaches to Thermodynamics of Site-Specific Protein-DNA Interactions
Thermodynamic Parameters from Hydrogen Exchange Measurements
Application of Pressure to Biochemical Equilibria: The Other Thermodynamic Variable
Molecular Volume
Hydrostatic and Osmotic Pressure as Tools to Study Macromolecular Recognition
Sedimentation Equilibrium as Thermodynamic Tool
Footprint Phenotypes: Structural Models of DNA-Binding Proteins from Chemical Modification Analysis of DNA
Low-Temperature Electrophoresis Methods
Use of Multiple Spectroscopic Methods to Monitor Equilibrium Unfolding of Proteins
Probing Structural and Physical Basis of Protein Energetics Linked to Protons and Salt
Evaluating Contribution of Hydrogen Bonding and Hydrophobic Bonding to Protein Folding
Analyzing Solvent Reorganization and Hydrophobicity
Simple Force Field for Study of Peptide and Protein Conformational Properties
Probes for Analysis of Stability of Different Variants of Aspartate Aminotransferase
Thermodynamic Approaches to Understanding Aspartate Transcarbamylase
On the Interpretation of Data from Isothermal Processes
Author Index
Subject Index
Table of Contents provided by Publisher. All Rights Reserved.

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Energetics of Biological Macromolecules

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Energetics of Biological Macromolecules

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Table of Contents

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