| Preface |
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ix | |
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1 | (20) |
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1 | (1) |
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2 | (1) |
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3 | (1) |
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4 | (3) |
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7 | (2) |
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9 | (1) |
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10 | (1) |
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11 | (4) |
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15 | (2) |
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Temperature Dependence of the Reaction Enthalpy |
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17 | (4) |
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18 | (1) |
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18 | (3) |
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21 | (20) |
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21 | (1) |
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Statement of the Second Law |
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22 | (2) |
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Calculation of the Entropy |
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24 | (2) |
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Third Law of Thermodynamics |
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26 | (1) |
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Molecular Interpretation of Entropy |
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27 | (1) |
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28 | (2) |
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30 | (3) |
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Pressure and Temperature Dependence of the Free Energy |
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33 | (2) |
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35 | (2) |
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Additions to the Free Energy |
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37 | (4) |
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37 | (4) |
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Applications of Thermodynamics to Biological Systems |
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41 | (30) |
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41 | (1) |
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42 | (5) |
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47 | (1) |
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Establishment of Membrane Ion Gradients by Chemical Reactions |
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48 | (2) |
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50 | (6) |
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56 | (3) |
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59 | (3) |
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62 | (4) |
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66 | (5) |
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68 | (1) |
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68 | (3) |
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71 | (23) |
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71 | (2) |
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73 | (2) |
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Determination of Rate Laws |
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75 | (3) |
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78 | (1) |
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79 | (4) |
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Temperature Dependence of Rate Constants |
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83 | (3) |
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Relationship Between Thermodynamics and Kinetics |
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86 | (2) |
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Reaction Rates Near Equilibrium |
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88 | (6) |
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91 | (1) |
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91 | (3) |
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Applications of Kinetics to Biological Systems |
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94 | (30) |
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94 | (1) |
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Enzyme Catalysis: The Michaelis--Menten Mechanism |
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94 | (5) |
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99 | (7) |
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Protein Tyrosine Phosphatase |
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106 | (3) |
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109 | (4) |
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DNA Melting and Renaturation |
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113 | (11) |
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119 | (1) |
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120 | (4) |
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Ligand Binding to Macromolecules |
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124 | (37) |
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124 | (1) |
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Binding of Small Molecules to Multiple Identical Binding Sites |
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124 | (3) |
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Macroscopic and Microscopic Equilibrium Constants |
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127 | (1) |
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Statistical Effects in Ligand Binding to Macromolecules |
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128 | (4) |
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Experimental Determination of Ligand Binding Isotherms |
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132 | (3) |
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Binding of Cro Repressor Protein to DNA |
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135 | (3) |
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Cooperativity in Ligand Binding |
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138 | (5) |
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143 | (4) |
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Kinetic Studies of Cooperative Binding |
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147 | (1) |
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148 | (6) |
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151 | (1) |
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152 | (2) |
| Appendixes |
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1. Standard Free Energies and Enthalpies of Formation at 298 K, 1 Atmosphere, pH 7, and 0.25 M Ionic Strength |
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154 | (2) |
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2. Standard Free Energy and Enthalpy Changes for Biochemical Reactions at 298 K, 1 Atmosphere, pH 7.0, pMg 3.0, and 0.25 M Ionic Strength |
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156 | (1) |
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3. Structures of the Common Amino Acids at Neutral pH |
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157 | (2) |
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4. Useful Constants and Conversion Factors |
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159 | (2) |
| Index |
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161 | |