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Quantitative Fundamentals of Molecular and Cellular Bioengineering [electronic resource].
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| 자료유형 | E-Book |
|---|---|
| 개인저자 | Wittrup, K. Dane. Tidor, Bruce. Hackel, Benjamin J. Sarkar, Casim A. |
| 서명/저자사항 | Quantitative Fundamentals of Molecular and Cellular Bioengineering[electronic resource]. |
| 발행사항 | Cambridge : MIT Press, 2020. |
| 형태사항 | 1 online resource (568 p.) |
| ISBN | 0262353970 9780262353977 |
| 일반주기 |
Description based upon print version of record.
Case Study 3-1 J. D. Stone, J. R. Cochran, and L. J. Stern. T-cell activation by soluble MHC oligomers can be described by a two-parameter binding model. Biophys. J. 81: 2547-2557 (2001). |
| 내용주기 | Intro -- Title Page -- Copyright -- Table of Contents -- Dedication -- Preface and Acknowledgments -- 1. Introduction to Biological Rate Processes -- 1.1. Biological Rate Processes -- 1.2. Why Develop a Model? -- 1.3. Mechanistic Model Formulation -- 1.4. Model Validation -- 1.4.1. Consistency with Experiment Is Necessary but Not Sufficient for a Model's Correctness -- 1.4.2. Comparison to Alternative Models -- 1.4.3. Prediction and Falsifiability -- 1.4.4. Parameter Sensitivity Analysis -- 1.5. Basic Themes in Rate Process Modeling -- 1.5.1. Steady State versus Equilibrium 1.5.2. Perturbations -- 1.5.3. Rate Forms -- 1.5.4. Characteristic Time and Length Scales -- Suggestions for Further Reading -- References -- 2. Noncovalent Binding Interactions -- 2.1. Kinetic Rate Constants -- 2.1.1. Typical Ranges for kon and koff -- 2.2. Thermodynamics -- 2.2.1. State Functions -- 2.2.2. Free Energy and Standard States -- 2.3. Energetic Contributions to Binding Affinity -- 2.3.1. Electrostatics -- 2.3.2. Hydrogen Bonding -- 2.3.3. van der Waals Interactions -- 2.3.4. Hydrophobic Effect -- 2.3.5. Deformation Energy and Entropy -- 2.4. Energetics of Protein Binding Interfaces 2.4.1. Thermodynamic Cycle Analysis -- Case Study 2-1 P. J. Carter, G. Winter, A. J. Wilkinson, and A. R. Fersht. The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus). Cell 38: 835-840 (1984). -- Case Study 2-2 Z. S. Hendsch and B. Tidor. Do salt bridges stabilize proteins? A continuum electrostatic analysis. Protein Sci. 3: 211-226 (1994). -- 2.5. Environmental Impacts on Binding Rate -- 2.5.1. Arrhenius Relationship and Transition State Theory -- 2.5.2. Electrostatic Effects on Binding Kinetics 2.6. Molecular Measurements: Light-Matter Interactions -- 2.6.1. Scattering -- 2.6.2. Absorbance -- 2.6.3. Fluorescence -- Case Study 2-3 L. Song, E. J. Hennink, I. T. Young, and H. J. Tanke. Photobleaching kinetics of fluorescein in quantitative fluorescence microscopy. Biophys. J. 68: 2588-2600 (1995). -- 2.7. Fluorescence Applications for Biomolecular Measurements -- 2.7.1. Biosynthetic Fluorescent Labeling -- Case Study 2-4 B. G. Reid and G. C. Flynn. Chromophore formation in green fluorescent protein. Biochemistry 36: 6786-6791 (1997). -- 2.7.2. Common Fluorophores for In Vitro Conjugation 2.7.3. Fluorescence Instrumentation -- Suggestions for Further Reading -- Problems -- References -- 3. Binding Equilibria and Kinetics -- 3.1. Equilibrium Monovalent Protein-Ligand Binding -- 3.1.1. Monovalent Binding Isotherm -- 3.1.2. Graphical Representations -- 3.2. Binding Kinetics -- 3.3. Multiple Binding Sites -- 3.3.1. Independent Sites -- 3.3.2. Cooperativity -- 3.3.3. Avidity and Effective Concentration -- 3.3.4. Equilibrium Bivalent Binding at Cell Surfaces |
| 요약 | A comprehensive presentation of essential topics for biological engineers, focusing on the development and application of dynamic models of biomolecular and cellular phenomena. |
| 일반주제명 | Science. SCIENCE / Life Sciences / Molecular Biology. Science. |
| 언어 | 영어 |
| 기타형태 저록 | Print version:Wittrup, K. DaneQuantitative Fundamentals of Molecular and Cellular BioengineeringCambridge : MIT Press,c20209780262042659 |
| 대출바로가기 | https://search.ebscohost.com/login.aspx?direct=true&scope=site&db=nlebk&db=nlabk&AN=2654327 |
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