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...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Sirotkin, Vladimir A. (Editor )
Formato: Electrónico eBook
Idioma:Inglés
Publicado: New York : Novinka, [2014]
Colección:Protein biochemistry, synthesis, structure, and cellular functions series.
Temas:
Water.
Solvation.
Proteins.
Eau.
Solvatation.
Protéines.
aquatic.
protein.
water (inorganic material)
SCIENCE > Chemistry > Inorganic.
Proteins
Solvation
Water
Acceso en línea:Texto completo

MARC

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245 0 0 |a Protein - water interactions :  |b a differential approach /  |c Vladimir A. Sirotkin, editor. 
264 1 |a New York :  |b Novinka,  |c [2014] 
264 4 |c ©2014 
300 |a 1 online resource. 
336 |a text  |b txt  |2 rdacontent 
337 |a computer  |b c  |2 rdamedia 
338 |a online resource  |b cr  |2 rdacarrier 
490 1 |a Protein biochemistry, synthesis, structure and cellular functions 
504 |a Includes bibliographical references and index. 
588 |a Description based on print version record. 
505 0 |a 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. 
505 8 |a 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. 
505 8 |a 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. 
505 8 |a 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. 
505 8 |a 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. 
520 |a 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. 
590 |a eBooks on EBSCOhost  |b EBSCO eBook Subscription Academic Collection - Worldwide 
650 0 |a Water. 
650 0 |a Solvation. 
650 0 |a Proteins. 
650 6 |a Eau. 
650 6 |a Solvatation. 
650 6 |a Protéines. 
650 7 |a aquatic.  |2 aat 
650 7 |a protein.  |2 aat 
650 7 |a water (inorganic material)  |2 aat 
650 7 |a SCIENCE  |x Chemistry  |x Inorganic.  |2 bisacsh 
650 7 |a Proteins  |2 fast 
650 7 |a Solvation  |2 fast 
650 7 |a Water  |2 fast 
700 1 |a Sirotkin, Vladimir A.,  |e editor. 
776 0 8 |i Print version:  |t Protein - water interactions  |d New York : Novinka, [2014]  |z 9781634630078 (pbk.)  |w (DLC) 2014950567 
830 0 |a Protein biochemistry, synthesis, structure, and cellular functions series. 
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994 |a 92  |b IZTAP 

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