Thermodynamics and Kinetics for the Biological Sciences

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Edition: 1st
Format: Paperback
Pub. Date: 2000-06-26
Publisher(s): Wiley-Interscience
List Price: $132.33

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Summary

Gain a working knowledge of thermodynamics and kinetics with a minimum of mathematics-a guide for individuals in the biological sciences An understanding of thermodynamics and kinetics is essential for researchers investigating molecular phenomena in diverse disciplines, including bioorganic chemistry, medicinal chemistry, biochemistry, pharmaceuticals, and biology. The use of these physical chemistry tools in the biological sciences has exploded over the past fifteen years, but the majority of works on thermodynamics and kinetics require mathematical expertise beyond that of many researchers in the field. Presenting a highly accessible introduction to thermodynamics and kinetics, Thermodynamics and Kinetics for the Biological Sciences employs a minimum of mathematics, assuming only a basic calculus background, while treating a wide range of topics in a logical and easy-to-follow style. All principles and concepts are clearly illustrated through the use of relevant applications and examples from the biological sciences, and explanations are further enhanced with problems and up-to-date references. Written by a world-renowned authority on biochemical kinetics, this remarkable book also features an easy-to-understand statistical development of entropy and a more extensive coverage of chemical kinetics and ligand binding to macromolecules than is usually found in books of this kind. Readers will acquire a working knowledge of thermodynamics and kinetics that they can readily apply to biological systems and use for exploring the scientific literature.

Author Biography

GORDON G. HAMMES, PhD, is University Distinguished Service Professor of Biochemistry at Duke University Medical Center, Durham, North Carolina, and Editor-in-Chief of the journal Biochemistry.

Table of Contents

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

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