Kooperativer Bibliotheksverbund

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Format: 1 online resource (142 p.)

ISBN: 1-63463-035-1

Series Statement: Protein biochemistry, synthesis, structure and cellular functions

Content: 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 the structure, stability, and functions of proteins. Knowledge of processes occurring upon hydration or dehydration of protein macromolecules is very important in biotechnological and pharmaceutical applications of proteins such as their use as biocatalysts, biosensors, and selective adsorbents. The

Note: Description based upon print version of record. , ""PROTEIN â€? WATER INTERACTIONS: A DIFFERENTIAL APPROACH""; ""PROTEIN â€? 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 Quantities""; ""References""; ""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 Measurements""; ""3.3. 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 â€? Water Mixtures""; ""Abstract""; ""1. Introduction""; ""2. Methodology""; ""3. Experimental""; ""3.1. Materials""; ""3.2. Calorimetry""; ""3.3. 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 Solvents""; ""4.2. 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"" , English

Additional Edition: ISBN 1-63463-007-6

Language: English