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Protein - water interactions : a differential approach /
This book is aimed at understanding which molecular parameters control the thermodynamics, structure, and functions of the protein-water systems. Proteins are one of the most important classes of biological molecules. Water binding (hydration or biological water) plays a crucial role in determining...
| Clasificación: | Libro Electrónico |
|---|---|
| Otros Autores: | |
| Formato: | Electrónico eBook |
| Idioma: | Inglés |
| Publicado: |
New York :
Novinka,
[2014]
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| Colección: | Protein biochemistry, synthesis, structure, and cellular functions series.
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| Temas: | |
| Acceso en línea: | Texto completo |
Tabla de Contenidos:
- PROTEIN
- WATER INTERACTIONS: A DIFFERENTIAL APPROACH; PROTEIN
- WATER INTERACTIONS: A DIFFERENTIAL APPROACH; Library of Congress Cataloging-in-Publication Data; Contents; Preface; Chapter 1: Analysis of Hydration of Binary Protein-Water Mixtures. Methodology; Abstract; 1. Introduction; 2. Methodology; 2.1. Excess Partial Quantities; 2.2. Excess Partial Volumes of Water and Proteins; 2.3. Excess Partial Heat Capacities of Water and Proteins; 2.4. Excess Partial Enthalpies; 2.4.1. Method 1; 2.4.2. Method 2; 2.5. Excess Partial Gibbs Energies; 2.6. Excess Partial Entropies.
- 2.7. Isosteric QuantitiesReferences; Chapter 2: A Study of the Excess Gibbs Energy of Ribonuclease A
- Water Mixtures; Abstract; Introduction; 2. Methodology; 2.1. Excess Partial Quantities; 2.2. Excess Partial Gibbs Energies; 3. Experimental Section; 3.1. Materials; 3.2. Water Sorption Measurements; 4. Results and Discussion; 4.1. Part 1. (W1 = 0-0.05); 4.2. Part 2. (W1 = 0.05-0.25); 4.3. Part 3. (W1 = 0.25-0.5); 4.4. Part 4. (W1> 0.5); References; Chapter 3: Analysis of Hydration of Ovalbumin by Densitometry; Abstract; 1. Introduction; 2. Methodology; 3. Experimental; 3.1. Materials.
- 3.2. Water Sorption Measurements3.3. Densitometry; 4. Results and Discussion; References; Chapter 4: Analysis of Hydration of Ovalbumin by Isothermal Calorimetry; Abstract; 1. Introduction; 2. Methodology; 2.1. Excess Partial Quantities; 2.2. Excess Partial Enthalpies; 3. Experimental; 3.1. Materials; 3.2. Water Sorption Measurements; 3.3. Calorimetry; 4. Results and Discussion; 4.1. Partial Enthalpies of Water and Ovalbumin; References; Chapter 5: A Study of the Heat Capacity of Ribonuclease A
- Water Mixtures; Abstract; 1. Introduction; 2. Methodology; 3. Experimental; 3.1. Materials.
- 3.2. Calorimetry3.3. Water Sorption Measurements; 4. Results and Discussion; 4.1. Regime 1. (w1=0-0.05).; 4.2. Regime 2 (w1=0.05-0.25); 4.3. Regime 3 (w1=0.25-0.5).; 4.4. Regime 4. (w1> 0.5).; Conclusion; References; Chapter 6: Effect of Water Solvation on the Heat Effects of Dehydration of Alpha-Chymotrypsin in Organic Solvents; Abstract; 1. Introduction; 2. Experimental Section; 2.1. Materials; 2.2. Calorimetry; 2.3. Water Content of Organic Solvents; 2.4. Enthalpies of Solvation of Water in Organic Solvents; 3. Methodology; 4. Results and Discussion.
- 4.1. Interaction Enthalpies of the Dried and Hydrated Enzyme with Organic Solvents4.2. Heat Effects of Dehydration of Chymotrypsin in Organic Solvents; Chapter 7: Analysis of the Organic Solvent Effect on the Hydration and Structure of Alpha-Chymotrypsin; Abstract; 1. Introduction; 2. Experimental; 2.1. Materials; 2.2. Thermodynamic Activity of Water; 2.3. Spectroscopic Measurements; 3. Results and Discussion; 3.1. Water sorption Isotherms; 3.2. Analysis and Band Assignment of Protein Infrared Spectra; 3.3. Effect of Acetonitrile on the Hydration and Structure of ( -Chymotrypsin.