Protein structure, stability, and interactions / edited by John W. Shriver. — New York : Humana Press, c2009. – (58.17/M592/v.490)

Contents

    Contents
    
    Preface v
    Contributors ix
    1 Microcalorimetry of Proteins and Their Complexes I
    2 Determining the Conformational Stability of a Protein Using Urea Denaturation Curves 41
    3 Defining the Stability of Multimeric Proteins 57
    4 Protein-Protein and Ligand-Protein Interactions Studied by Analytical Ultracentrifugation 83
    5 Monitoring Molecular Interactions by NMR 115
    6 Ligand-Binding Interactions and Stability 135
    7 A Method for Direct Measurement of Protein Stability In Vivo 165
    8 Quantifying the Roles of Water and Solutes (Denaturants， Osmolytes， and Hofmeister Salts) in Protein and Model Processes Using the Solute Partitioning Mode 179
    9 Molecular Crowding and Solvation: Direct and Indirect Impact on Protein Reactions 195
    10 Defining the Role of Salt Bridges in Protein Stability
    11 Protein Stabilization by the Rational Design of Surface Charge-Charge Interactions 261
    12 NMRAnalysis of Native-State Protein Conformational Flexibility by Hydrogen Exchange 285
    13 Single-Molecule Fluorescence Studies of Protein Folding 311
    14 Experimental Characterization of the Denatured State Ensemble of Proteins 339
    Index 353