5
1
2901118859000
Preface v
Thermodynamics 1
Heat, Work, and Energy 3
Introduction 3
Temperature 4
Heat 5
Work 6
Definition of Energy 9
Enthalpy 11
Standard States 12
Calorimetry 13
Reaction Enthalpies 16
Temperature Dependence of the Reaction Enthalpy 18
References 19
Problems 20
Entropy and Free Energy 22
Introduction 22
Statement of the Second Law 23
Calculation of the Entropy 25
Third Law of Thermodynamics 27
Molecular Interpretation of Entropy 28
Free Energy 29
Chemical Equilibria 31
Pressure and Temperature Dependence of the Free Energy 34
Phase Changes 36
Additions to the Free Energy 38
Problems 39
Applications of Thermodynamics to Biological Systems 42
Biochemical Reactions 42
Metabolic Cycles 44
Direct Synthesis of ATP 48
Establishment of Membrane Ion Gradients by Chemical Reactions 49
Protein Structure 51
Protein Folding 57
Nucleic Acid Structures 60
DNA Melting 63
RNA 67
References 68
Problems 69
Chemical Kinetics 73
Principles of Chemical Kinetics 75
Introduction 75
Reaction Rates 77
Determination of Rate Laws 79
Radioactive Decay 82
Reaction Mechanisms 83
Temperature Dependence of Rate Constants 86
Relationship between Thermodynamics and Kinetics 90
Reaction Rates Near Equilibrium 91
References 94
Problems 94
Applications of Kinetics to Biological Systems 97
Introduction 97
Enzyme Catalysis: The Michaelis-Menten Mechanism 97
[alpha]-Chymotrypsin 102
Protein Tyrosine Phosphatase 109
Ribozymes 112
DNA Melting and Renaturation 116
References 122
Problems 123
Spectroscopy 127
Fundamentals of Spectroscopy 129
Introduction 129
Quantum Mechanics 130
Particle in a Box 133
Properties of Waves 137
References 141
Problems 141
X-ray Crystallography 143
Introduction 143
Scattering of X rays by a Crystal 144
Structure Determination 146
Neutron Diffraction 150
Nucleic Acid Structure 151
Protein Structure 153
Enzyme Catalysis 155
References 157
Problems 157
Electronic Spectra 159
Introduction 159
Absorption Spectra 160
Ultraviolet Spectra of Proteins 162
Nucleic Acid Spectra 164
Prosthetic Groups 165
Difference Spectroscopy 167
X-ray Absorption Spectroscopy 170
Fluorescence and Phosphorescence 171
RecBCD: Helicase Activity Monitored by Fluorescence 174
Fluorescence Energy Transfer: A Molecular Ruler 175
Application of Energy Transfer to Biological Systems 177
Dihydrofolate Reductase 180
References 181
Problems 182
Circular Dichroism, Optical Rotary Dispersion, and Fluorescence Polarization 186
Introduction 186
Optical Rotary Dispersion 188
Circular Dichroism 189
Optical Rotary Dispersion and Circular Dichroism of Proteins 190
Optical Rotation and Circular Dichroism of Nucleic Acids 192
Small Molecule Binding to DNA 194
Protein Folding 196
Interaction of DNA with Zinc Finger Proteins 199
Fluorescence Polarization 201
Integration of HIV Genome into Host Genome 202
[alpha]-ketoglutarate Dehydrogenase 203
References 206
Problems 206
Vibrations in Macromolecules 210
Introduction 210
Infrared Spectroscopy 212
Raman Spectroscopy 213
Structure Determination with Vibrational Spectroscopy 215
Resonance Raman Spectroscopy 218
Structure of Enzyme-Substrate Complexes 220
References 221
Problems 221
Principles of Nuclear Magnetic Resonance and Electron Spin Resonance 223
Introduction 223
NMR Spectrometers 226
Chemical Shifts 227
Spin-Spin Splitting 229
Relaxation Times 232
Multidimensional NMR 234
Magnetic Resonance Imaging 240
Electron Spin Resonance 241
References 244
Problems 244
Applications of Magnetic Resonance to Biology 248
Introduction 248
Regulation of DNA Transcription 248
Protein-DNA Interactions 251
Dynamics of Protein Folding 252
RNA Folding 254
Lactose Permease 257
Conclusion 260
References 260
Special Topics 263
Ligand Binding to Macromolecules 265
Introduction 265
Binding of Small Molecules to Multiple Identical Binding Sites 265
Macroscopic and Microscopic Equilibrium Constants 268
Statistical Effects in Ligand Binding to Macromolecules 269
Experimental Determination of Ligand Binding Isotherms 273
Binding of Cro Repressor Protein to DNA 276
Cooperativity in Ligand Binding 279
Models for Cooperativity 281
Kinetic Studies of Cooperative Binding 287
Allosterism 289
References 292
Problems 292
Hydrodynamics of Macromolecules 295
Introduction 295
Frictional Coefficient 295
Diffusion 298
Centrifugation 301
Velocity Sedimentation 302
Equilibrium Centrifugation 305
Preparative Centrifugation 307
Density Centrifugation 307
Viscosity 309
Electrophoresis 310
Peptide-Induced Conformational Change of a Major Histocompatibility Complex Protein 312
Ultracentrifuge Analysis of Protein-DNA Interactions 315
References 316
Problems 316
Mass Spectrometry 320
Introduction 320
Mass Analysis 320
Tandem Mass Spectrometry (MS/MS) 323
Ion Detectors 324
Ionization of the Sample 325
Sample Preparation/Analysis 327
Proteins and Peptides 329
Protein Folding 331
Other Biomolecules 334
References 335
Problems 335
Appendices 337
Useful Constants and Conversion Factors 339
Structures of the Common Amino Acids at Neutral pH 340
Common Nucleic Acid Components 342
Standard Free Energies and Enthalpies of Formation at 298 K, 1 atm, pH 7, and 0.25 M Ionic Strength 343
Standard Free Energy and Enthalpy Changes for Biochemical Reactions at 298 K, 1 atm, pH 7.0, pMg 3.0, and 0.25 M Ionic Strength 345
Index 347
Physical Chemistry for the Biological Sciences / Edition 2 available in Hardcover, eBook
Physical Chemistry for the Biological Sciences / Edition 2
by Gordon G. Hammes
Gordon G. Hammes
Physical Chemistry for the Biological Sciences / Edition 2
by Gordon G. Hammes
Gordon G. Hammes
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Overview
Physical Chemistry for the Biological Sciences is an excellent resource for biochemistry and biology/health science professionals and students who need a basic understanding of thermodynamics, kinetics, hydrodynamics of macromolecules, and spectroscopy in order to explore molecular structure and chemical reactions. Approachable, yet thorough, the book presents physical chemistry in conceptual terms with a minimum of mathematics. Providing the basic knowledge and tools that every biologist should have to understand the quantitative interpretation of biological phenomena, it covers: Fundamentals of thermodynamics and chemical kinetics, Fundamentals of spectroscopy and structure determination, Ligand binding to macromolecules, hydrodynamics, and mass spectrometry. All techniques and concepts are clearly illustrated with relevant applications and examples from the biological sciences. Problems at the end of each chapter reinforce the principles. This is a succinct reference for practitioners, including bioorganic chemists, medicinal chemists, biochemists, pharmaceutical chemists, biologists, and professionals in fields such as pharmaceuticals, agriculture, and biotechnology. It's also an excellent textbook for graduate and upper-level undergraduate students in biochemistry, biology, and related fields.
About the Author:
Gordon G. Hammes, PhD, is University Distinguished Service Professor of Biochemistry at Duke University Medical Center in Durham, North Carolina
Product Details
ISBN-13: | 2901118859000 |
---|---|
Publication date: | 04/20/2015 |
Pages: | 504 |
Product dimensions: | 6.50(w) x 1.50(h) x 9.50(d) |
About the Author
Gordon G. Hammes, PhD, is the Distinguished Service Professor of Biochemistry Emeritus at Duke University. He is a member of the National Academy of Sciences and the American Academy of Arts and Sciences, and has received several national awards, including the American Chemical Society Award in Biological Chemistry and the American Society for Biochemistry and Molecular Biology William C. Rose Award. Dr. Hammes was Editor of the journal Biochemistry from 1992-2003.Sharon Hammes-Schiffer, PhD, is the Swanlund Professor of Chemistry at the University of Illinois at Urbana-Champaign. She is a fellow of the American Physical Society, the American Chemical Society, the Biophysical Society, and the American Association for the Advancement of Science. She is a member of the American Academy of Arts and Sciences, the National Academy of Sciences, and the International Academy of Quantum Molecular Science. Dr. Hammes-Schiffer has served as the Deputy Editor of The Journal of Physical Chemistry B and is currently the Editor-in-Chief of Chemical Reviews.
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Table of Contents
Preface v
Thermodynamics 1
Heat, Work, and Energy 3
Introduction 3
Temperature 4
Heat 5
Work 6
Definition of Energy 9
Enthalpy 11
Standard States 12
Calorimetry 13
Reaction Enthalpies 16
Temperature Dependence of the Reaction Enthalpy 18
References 19
Problems 20
Entropy and Free Energy 22
Introduction 22
Statement of the Second Law 23
Calculation of the Entropy 25
Third Law of Thermodynamics 27
Molecular Interpretation of Entropy 28
Free Energy 29
Chemical Equilibria 31
Pressure and Temperature Dependence of the Free Energy 34
Phase Changes 36
Additions to the Free Energy 38
Problems 39
Applications of Thermodynamics to Biological Systems 42
Biochemical Reactions 42
Metabolic Cycles 44
Direct Synthesis of ATP 48
Establishment of Membrane Ion Gradients by Chemical Reactions 49
Protein Structure 51
Protein Folding 57
Nucleic Acid Structures 60
DNA Melting 63
RNA 67
References 68
Problems 69
Chemical Kinetics 73
Principles of Chemical Kinetics 75
Introduction 75
Reaction Rates 77
Determination of Rate Laws 79
Radioactive Decay 82
Reaction Mechanisms 83
Temperature Dependence of Rate Constants 86
Relationship between Thermodynamics and Kinetics 90
Reaction Rates Near Equilibrium 91
References 94
Problems 94
Applications of Kinetics to Biological Systems 97
Introduction 97
Enzyme Catalysis: The Michaelis-Menten Mechanism 97
[alpha]-Chymotrypsin 102
Protein Tyrosine Phosphatase 109
Ribozymes 112
DNA Melting and Renaturation 116
References 122
Problems 123
Spectroscopy 127
Fundamentals of Spectroscopy 129
Introduction 129
Quantum Mechanics 130
Particle in a Box 133
Properties of Waves 137
References 141
Problems 141
X-ray Crystallography 143
Introduction 143
Scattering of X rays by a Crystal 144
Structure Determination 146
Neutron Diffraction 150
Nucleic Acid Structure 151
Protein Structure 153
Enzyme Catalysis 155
References 157
Problems 157
Electronic Spectra 159
Introduction 159
Absorption Spectra 160
Ultraviolet Spectra of Proteins 162
Nucleic Acid Spectra 164
Prosthetic Groups 165
Difference Spectroscopy 167
X-ray Absorption Spectroscopy 170
Fluorescence and Phosphorescence 171
RecBCD: Helicase Activity Monitored by Fluorescence 174
Fluorescence Energy Transfer: A Molecular Ruler 175
Application of Energy Transfer to Biological Systems 177
Dihydrofolate Reductase 180
References 181
Problems 182
Circular Dichroism, Optical Rotary Dispersion, and Fluorescence Polarization 186
Introduction 186
Optical Rotary Dispersion 188
Circular Dichroism 189
Optical Rotary Dispersion and Circular Dichroism of Proteins 190
Optical Rotation and Circular Dichroism of Nucleic Acids 192
Small Molecule Binding to DNA 194
Protein Folding 196
Interaction of DNA with Zinc Finger Proteins 199
Fluorescence Polarization 201
Integration of HIV Genome into Host Genome 202
[alpha]-ketoglutarate Dehydrogenase 203
References 206
Problems 206
Vibrations in Macromolecules 210
Introduction 210
Infrared Spectroscopy 212
Raman Spectroscopy 213
Structure Determination with Vibrational Spectroscopy 215
Resonance Raman Spectroscopy 218
Structure of Enzyme-Substrate Complexes 220
References 221
Problems 221
Principles of Nuclear Magnetic Resonance and Electron Spin Resonance 223
Introduction 223
NMR Spectrometers 226
Chemical Shifts 227
Spin-Spin Splitting 229
Relaxation Times 232
Multidimensional NMR 234
Magnetic Resonance Imaging 240
Electron Spin Resonance 241
References 244
Problems 244
Applications of Magnetic Resonance to Biology 248
Introduction 248
Regulation of DNA Transcription 248
Protein-DNA Interactions 251
Dynamics of Protein Folding 252
RNA Folding 254
Lactose Permease 257
Conclusion 260
References 260
Special Topics 263
Ligand Binding to Macromolecules 265
Introduction 265
Binding of Small Molecules to Multiple Identical Binding Sites 265
Macroscopic and Microscopic Equilibrium Constants 268
Statistical Effects in Ligand Binding to Macromolecules 269
Experimental Determination of Ligand Binding Isotherms 273
Binding of Cro Repressor Protein to DNA 276
Cooperativity in Ligand Binding 279
Models for Cooperativity 281
Kinetic Studies of Cooperative Binding 287
Allosterism 289
References 292
Problems 292
Hydrodynamics of Macromolecules 295
Introduction 295
Frictional Coefficient 295
Diffusion 298
Centrifugation 301
Velocity Sedimentation 302
Equilibrium Centrifugation 305
Preparative Centrifugation 307
Density Centrifugation 307
Viscosity 309
Electrophoresis 310
Peptide-Induced Conformational Change of a Major Histocompatibility Complex Protein 312
Ultracentrifuge Analysis of Protein-DNA Interactions 315
References 316
Problems 316
Mass Spectrometry 320
Introduction 320
Mass Analysis 320
Tandem Mass Spectrometry (MS/MS) 323
Ion Detectors 324
Ionization of the Sample 325
Sample Preparation/Analysis 327
Proteins and Peptides 329
Protein Folding 331
Other Biomolecules 334
References 335
Problems 335
Appendices 337
Useful Constants and Conversion Factors 339
Structures of the Common Amino Acids at Neutral pH 340
Common Nucleic Acid Components 342
Standard Free Energies and Enthalpies of Formation at 298 K, 1 atm, pH 7, and 0.25 M Ionic Strength 343
Standard Free Energy and Enthalpy Changes for Biochemical Reactions at 298 K, 1 atm, pH 7.0, pMg 3.0, and 0.25 M Ionic Strength 345
Index 347
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