Thermodynamic Data for Biochemistry and Biotechnology (Paperback, Softcover Repri)

Section I Introduction.- 1 Present and Future Uses and a Bit of History.- 1 Some Early History.- 2 Acids, Bases, and Oxidation-Reduction Equilibria.- 3 Thermodynamics of Major Metabolic Processes.- 4 Thermodynamics of Amino Acids and Proteins: Electrostatic and Hydrophobic Interactions.- 5 Thermodynamics of Ligand Binding to Macromolecules.- 6 The Contributions of this Book.- References.- Appendix: Physical Quantities, Units, and Conversion Factors.- Section II Nonreacting Systems.- 2 Partial Molar Volumes of Biochemical Model Compounds in Aqueous Solution.- 1 Introduction.- 2 Definitions.- 3 Extrapolation to Infinite Dilution.- 4 Tabulation of the Experimental Data.- 5 Alcohols, Polyols, and Phenols.- 6 Ethers, Ketones, and Aldehydes.- 7 Carboxylic Acids, Sodium Carboxylates, and Esters.- 8 Amines, Amides, and Ureas.- 9 Carbohydrates.- 10 Amino Acids and Low Molar Mass Proteins.- 11 Group Additivity of Partial Molar Volumes.- 12 Models Based on van der Waals Volumes.- 13 Conclusions.- 14 Addendum.- References.- 3 Specific Volumes of Biological Macromolecules and Some Other Molecules of Biological Interest.- 1 Introduction.- 2 Definitions.- 2.1 Volume and Density.- 2.2 Specific Volumes.- 3 Determination of Specific Volumes.- 3.1 Calculation.- 3.1.1 Traube's Additivity Principle.- 3.1.2 Native Nonconjugated Proteins.- 3.1.3 Native Conjugated Proteins.- 3.1.4 Protein Complexes.- 3.1.5 Denatured Proteins.- 3.2 Experimental Determination.- 3.2.1 Methods.- 3.2.2 Digital Densimetry.- 4 Tabulation and Interpretation of Data.- 4.1 Specific Volumes.- 4.1.1 Small Molecules.- 4.1.2 Polyamino Acids and Peptides.- 4.1.3 Native Nonconjugated Proteins.- 4.1.4 Native Conjugated Proteins.- 4.1.5 Denatured Proteins.- 4.1.6 Polysaccharides.- 4.1.7 Lipids, Membranes, and Micelles.- 4.1.8 Polynucleotides and Nucleic Acids.- 4.2 Specific Volume Changes.- 4.2.1 Proteins.- 4.2.1.1 Protein Concentration.- 4.2.1.2 Temperature.- 4.2.1.3 Aging, Thermal Denaturation.- 4.2.1.4 Acid and Alkaline Denaturation.- 4.2.1.5 Different Buffers.- 4.2.1.6 Addition of Salts.- 4.2.1.7 Addition of Sugars of Polyols.- 4.2.1.8 Addition of Denaturants.- 4.2.1.9 Binding of Specific Ligands.- 4.2.2 Other Substances.- 5 Conclusions.- 6 Tables.- References.- 4 Partial Molar Compressibilities of Organic Solutes in Water.- 1 Introduction.- 2 Definitions.- 3 Tabulation of Experimental Results.- 4 Alcohols, Diols, and Ethers.- 5 Carboxylic Acids and Sodium Carboxylates.- 6 Amines, Amides, and Ureas.- 7 Carbohydrates.- 8 Amino Acids and Dipeptides.- 9 Proteins.- 10 Nucleobases and Nucleosides.- 11 Summary.- References.- 5 Heat Capacities of Biological Macromolecules.- 1 Introduction.- 2 Calorimetric Measurements.- 3 Experimental Results.- 3.1 Heat Capacity and Thermodynamic Properties of Amino Acid Residues over the Temperature Range 1.5-350 K.- 3.2 Heat Capacity and Thermodynamic Properties of Polypeptides over the Temperature Range 1.5-300 K.- 3.3 Heat Capacity and Thermodynamic Properties of Globular Proteins over the Temperature Range 10-350 K.- 3.4 Thermodynamic Properties of Fibrous Collagen in the Helical and Coil States at Temperatures 4-400 K.- 3.5 Heat Capacity of DNA.- 4 Concluding Remarks.- References.- 6 Thermodynamics of Carbohydrate Monomers and Polymers in Aqueous Solution.- 1 Introduction.- 2 Rationale for Concentration Dependence.- 3 Experimental Data for Simple Carbohydrates in Solution.- 4 Molecular Calculations of Thermodynamic Properties.- 4.1 Conformational Properties.- 4.2 Comparison of Experimental Data with Those from Energy Calculations.- 5 Inclusion Complexes.- 5.1 Cyclodextrin Complexes.- 5.2 Energetics of the Amylose-Iodine Complex.- 6 Ionic Polysaccharides.- 6.1 Premise.- 6.2 The Polyelectrolytic Contrast Effect.- 6.3 Enthalpies of Dilution in Water.- 6.4 Enthalpies of Protonation of Carboxylated Polysaccharides.- 6.5 Enthalpy of Mixing with Ions.- 7 Conclusions.- References.- Section III Interactions in Solution.- 7 Thermodynamic Data for Protein