Biothermodynamics. Part A (2009)

• Record Type: Book
• Further Information: Note: Edited by Michael L. Johnson, Jo M. Holt and Gary K. Ackers.
• Other Names: Johnson, Michael L, 1947-; Holt, Jo M; Ackers, Gary K
• Contents: Front Cover; Methods in Enzymology Biothermodynamics, Part A; Copyright Page; Contents; Contributors; Preface; Volumes in Series; Chapter 1: Practical Approaches to Protein Folding and Assembly: Spectroscopic Strategies in Thermodynamics and Kinetics; 1. Introduction; 2. Equilibrium Unfolding; 3. Measuring Folding Kinetics; References; Chapter 2: Using Thermodynamics to Understand Progesterone Receptor Function: Method and Theory; 1. Introduction; 2. Assessing Protein Functional and Structural Homogeneity; 3. Dissecting Linked Assembly Reactions. 4. Analysis and Dissection of Natural Promoters5. Measuring the Energetics of Coactivator Recruitment; 6. Correlation to Biological Function; 7. Conclusions and Future Directions; Acknowledgments; References; Chapter 3: Direct Quantitation of Mg2+-RNA Interactions by Use of a Fluorescent Dye; 1. Introduction; 2. General Principles; 3. Ion-Binding Properties of HQS; 4. Preparation of Solutions and Reagents; 5. Instrumentation and Data Collection Protocols; 6. Data Analysis; 7. Controls and Further Considerations; Acknowledgments; References. Chapter 4: Analysis of Repeat-Protein Folding Using Nearest-Neighbor Statistical Mechanical Models1. Historical Overview of Ising Models and Motivation for the Present Review; 2. Linear Repeat Proteins and Their Connection to Linear Ising Models; 3. Formulating a Homopolymer Partition Function and the Zipper Approximation; 4. Matrix Approach: Homopolymers; 5. Matrix Approach: Heteropolymers; 6. Solvability Criteria for Ising Models Applied to Repeat-Protein Folding; 7. Matrix Homopolymer Analysis of Consensus TPR Folding; 8. Matrix Heteropolymer Analysis of Consensus Ankyrin Repeat Folding. 9. Summary and Future DirectionsAcknowledgments; References; Chapter 5: Isothermal Titration Calorimetry: General Formalism using Binding Polynomials; 1. Introduction; 2. The Binding Polynomial; 3. Microscopic Constants and Cooperativity; 4. Independent or Cooperative Binding?; 5. Analysis of ITC Data using Binding Polynomials; 6. A Typical Case: Macromolecule with Two Ligand-Binding Sites; 7. Data Analysis; 8. Data Interpretation; 9. An Experimental Example; 10. Experimental Situations from the Literature; 11. Macromolecule with Three Ligand-Binding Sites; 12. Conclusions; Appendix. AcknowledgmentsReferences; Chapter 6: Kinetic and Equilibrium Analysis of the Myosin ATPase; 1. Introduction; 2. Reagents and Equipment used for all Assays; 3. Steady-State ATPase Activity of Myosin; 4. Steady-State Measurement of Actomyosin Binding Affinities; 5. Transient Kinetic Analysis of the Individual ATPase Cycle Transitions; 6. Kinetic Simulations; Acknowledgments; References; Chapter 7: The Hill Coefficient: Inadequate Resolution of Cooperativity in Human Hemoglobin; 1. Introduction; 2. Cooperativity and Intrinsic Binding; 3. The Macroscopic Binding Isotherm; 4. The Hill Coefficient.
• Publisher Details: Amsterdam Boston San Diego, CA : Elsevier Academic Press
• Publication Date: 2009
• Extent: 1 online resource (xliii, 466 pages), illustrations
• Subjects: 572/.436; Protein folding; Thermodynamics; Protein binding; Protein-protein interactions; Thermodynamics; Protein Binding; Protein Array Analysis; Thermodynamics; SCIENCE -- Life Sciences -- Biochemistry; Protein binding; Protein folding; Protein-protein interactions; Thermodynamics; Electronic books
• Languages: English
• ISBNs: 9780080923406; 0080923402; 9780123745965; 0123745969
• Notes: Note: Includes bibliographical references and indexes.; Note: Print version record.
• Access Rights: Legal Deposit; Only available on premises controlled by the deposit library and to one user at any one time; The Legal Deposit Libraries (Non-Print Works) Regulations (UK).
• Access Usage: Restricted: Printing from this resource is governed by The Legal Deposit Libraries (Non-Print Works) Regulations (UK) and UK copyright law currently in force.