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  ▼a  610.284

• 100

  ▼a  Wittrup, K. Dane.

• 245

  ▼a  Quantitative Fundamentals of Molecular and Cellular Bioengineering
  ▼h  [electronic resource].

• 260

  ▼a  Cambridge:
  ▼b  MIT Press,
  ▼c  2020.

• 300

  ▼a  1 online resource (568 p.).

• 500

  ▼a  Description based upon print version of record.

• 500

  ▼a  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).

• 505

  ▼a  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

• 505

  ▼a  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

• 505

  ▼a  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

• 505

  ▼a  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

• 505

  ▼a  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

• 520

  ▼a  A comprehensive presentation of essential topics for biological engineers, focusing on the development and application of dynamic models of biomolecular and cellular phenomena.

• 650

  ▼a  Science.

• 650

  ▼a  SCIENCE / Life Sciences / Molecular Biology.
  ▼2  bisacsh

• 650

  ▼a  Science.
  ▼2  fast
  ▼0  (OCoLC)fst01108176

• 655

  ▼a  Electronic books.

• 700

  ▼a  Tidor, Bruce.

• 700

  ▼a  Hackel, Benjamin J.

• 700

  ▼a  Sarkar, Casim A.

• 776

  ▼i  Print version:
  ▼a  Wittrup, K. Dane
  ▼t  Quantitative Fundamentals of Molecular and Cellular Bioengineering.
  ▼d  Cambridge : MIT Press,c2020,
  ▼z  9780262042659

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