Ribonucleases. Pt. A [electronic resource] / edited by Allen W. Nicholson
- Published:
- San Diego : Academic Press, [2001]
- Copyright Date:
- ©2001
- Physical Description:
- xxxvi, 734 pages : illustrations ; 24 cm.
- Additional Creators:
- Nicholson, Allen W.
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- License restrictions may limit access.
- Contents:
- Machine generated contents note: 1.Measurement and Analysis of Equilibrium Binding Titrations: A Beginner's Guide / Dorothy Beckett -- 1.Material Requirements for Binding Measurements -- 2.Monitoring a Binding Reaction -- 3.The Binding Equation and Its Relationship to Binding Measurements -- 4.Plotting and Analysis of Binding Data -- 5.Protein Concentration Is Important: Equilibrium Versus Stoichiometric Conditions -- 6.When Are Total and Free Ligand Concentrations Equal? -- 7.Deviations from Simple Binding -- References -- 2.Macromolecular Competition Titration Method: Accessing Thermodynamics of the Unmodified Macromolecule-Ligand Interactions Through Spectroscopic Titrations of Fluorescent Analogs / Maria J. Jezewska -- 1.Introduction -- 2.A Single Titration Curve: Some Simple Considerations of Possible Pitfalls -- 3.Quantitative Equilibrium Spectroscopic Titrations: Thermodynamic Bases -- 4.Nucleotide Binding to the RepA Protein of Plasmid RSF1010 -- 5.Applying the Statistical Thermodynamic Model for the Nucleotide Binding to the RSF1010 RepA Protein Hexamer -- 6.Empirical Function Approach -- 7.MCT Method: General Considerations -- 8.Application of the MCT Method to the Base Specificity Problem in ASFV Pol X-ssDNA System -- 9.Application of MCT Method to Protein-ssDNA Lattice Binding Systems -- 10.Quantitative Analysis of the Binding of the E. coli DnaB Helicase to Unmodified Nucleic Acids Using the MCT Method -- 11.Direct Analysis of the Experimental Isotherm of Protein Ligand Binding to Two Competing Nucleic Acid Lattices -- 12.Using a Single Concentration of a Nonfluorescent Unmodified Nucleic Acid -- 13.Using Short Fluorescent Oligonucleotides in Competition with the Polymer Nucleic Acid -- 14.Conclusions -- Acknowledgments -- References -- 3.Analysis of PKR-RNA Interactions by Sedimentation Velocity / James L. Cole -- 1.Introduction -- 2.Reagents and Cells -- 3.Experimental Design -- 4.Examples -- 5.Conclusions -- Acknowledgments -- References -- 4.Structural and Thermodynamic Analysis of PDZ-Ligand Interactions / Ernesto J. Fuentes -- 1.Introduction -- 2.Structural Studies of the Tiam I PDZ Domain -- 3.Fluorescence Anisotropy Methods for Measuring the Energetics of PDZ-Ligand Interactions -- 4.Double-Mutant Cycle Analysis of PDZ-Binding Pockets -- 5.Peptide Evolution as a Tool for Probing PDZ Specificity -- 6.Conclusions -- Acknowledgments -- References -- 5.Thermodynamic Analysis of Metal Ion-Induced Protein Assembly / Deborah G. Conrady -- 1.Introduction -- 2.Linked Equilibria---General Concepts -- 3.Experimental Approaches---Analytical Ultracentrifugation -- 4.Summary -- Acknowledgments -- References -- 6.Thermodynamic Dissection of Colicin Interactions / Colin Kleanthous -- 1.Introduction -- 2.DNase Domain-Immunity Protein Interactions -- 3.Receptor Binding -- 4.Mapping Binding Epitopes and Signaling Networks -- 5.Discussion -- References -- 7.Energetics of Src Homology Domain Interactions in Receptor Tyrosine Kinase-Mediated Signaling / Stefan T. Arold -- 1.Introduction -- 2.Interactions of Src Homology 2 Domains -- 3.Recognition by the "Two-Pinned Plug" -- 4.Recognition by the β-Turn Motif -- 5.Selectivity Versus Specificity for SH2 Domain Interactions -- 6.Proline Sequence-Recognition Domains -- 7.Interactions of SH3 Domains -- 8.What Constitutes Specificity in SH3 Domain Interactions? -- 9.Selectivity in SH3 Domain Interactions -- 10.Interactions Through Multiple Domains -- 11.Conclusions -- References -- 8.Structural and Functional Energetic Linkages in Allosteric Regulation of Muscle Pyruvate Kinase / Petr Herman -- 1.Introduction -- 2.General Principles of Linked Multiequilibria Reactions -- 3.Functional Energetic Linkages in Allosteric Regulation of Rabbit Muscle Pyruvate Kinase -- 4.Functional Linkage Through Steady-State Kinetics -- 5.Structural Perturbations by Ligands -- 6.Functional Linkage Scheme of Allostery for RMPK -- 7.Functional Linkage Through Ligand Binding Measurements -- 8.Protein Structural Dynamics---Amid Hydrogen Exchange Monitored by FT-IR (HX-FT-IR) -- 9.Probing Interfacial Interactions -- 10.Summary Statement -- Acknowledgments -- References -- 9.Analysis of Free Energy Versus Temperature Curves in Protein Folding and Macromolecular Interactions / Chin-Chi Liu -- 1.Stability Curves = Gibbs-Helmholtz Curves = ΔG Versus Temperature -- 2.Analysis of ΔG Versus Temperature in Protein Folding -- 3.Using Stability Curves to Compare Mesophilic and Thermophilic Protein Pairs -- 4.Temperature Dependence of Folding Enthalpies and Entropies -- 5.Analysis of ΔG Versus Temperature Data in Macromolecular Interactions -- 6.Fitting ΔH and ΔG Versus Temperature for a ΔΔCp -- 7.Examples of Potential Consequences of a Small ΔΔCp -- References -- 10.Application of the Sequential n-Step Kinetic Mechanism to Polypeptide Translocases / Burki Rajendar -- 1.Introduction -- 2.Single-Turnover Fluorescence Stopped-Flow Method to Monitor Polypeptide Translocation -- 3.Application of the Sequential n-Step Mechanism -- 4.Concluding Remarks -- Acknowledgments -- References -- 11.A Coupled Equilibrium Approach to Study Nucleosome Thermodynamics / Karolin Luger -- 1.Introduction -- 2.Salt-Mediated Nucleosome (Dis)Assembly -- 3.A Chaperone-Mediated Coupled Approach to Nucleosome Thermodynamics -- 4.Experimental Setup and Considerations -- 5.Data Analysis and Theory -- 6.Summary and Implications -- References -- 12.Quantitative Methods for Measuring DNA Flexibility In Vitro and In Vivo / L. James Maher III -- 1.Introduction -- 2.DNA Polymer Theory -- 3.Ligase-Catalyzed DNA Cyclization Kinetics In Vitro -- 4.In Vivo Analysis of E. coli lac Repression Loops -- Acknowledgments -- References.
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- ISBN:
- 9780121822422 (alk. paper)
0121822427 (alk. paper) - Bibliography Note:
- Includes bibliographical references and indexes.
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