[下载]由wiley公司出版的酶学(Enzymes)第二版
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1.内容：Enzymes (Second Edition)(英文)
2.格式：PDF
3.作者：Robert A. Copeland
4.大小：6MB
5.出版社：2000 by Wiley-VCH, Inc.
7.简介：见下
本书经我在本论坛里没有找到有上传的，与大家共享。原先在FTP资源区，经老赵提醒放在专业区，由于好几位战友PM我要这本书，现重新在专业区申请！
下载目录在 /基础医学区/蛋白质技术专业组/pub/
1 A Brief History of Enzymology 1
1.1 Enzymes in Antiquity / 2
1.2 Early Enzymology / 3
1.3 The Development of Mechanistic Enzymology / 4
1.4 Studies of Enzyme Structure / 5
1.5 Enzymology Today / 7
1.6 Summary / 8
References and Further Reading / 10
2 Chemical Bonds and Reactions in Biochemistry 11
2.1 Atomic and Molecular Orbitals / 11
2.2 Thermodynamics of Chemical Reactions / 23
2.3 Acid—Base Chemistry / 29
2.4 Noncovalent Interactions in Reversible Binding / 32
2.5 Rates of Chemical Reactions / 35
2.6 Summary / 41
References and Further Reading / 41
3 Structural Components of Enzymes 42
3.1 The Amino Acids / 42
3.2 The Peptide Bond / 53
3.3 Amino Acid Sequence or Primary Structure / 55
3.4 Secondary Structure / 57
3.5 Tertiary Structure / 62
vii
3.6 Subunits and Quaternary Structure / 65
3.7 Cofactors in Enzymes / 68
3.8 Summary / 71
References and Further Reading / 74
4 Protein‒Ligand Binding Equilibria 76
4.1 The Equilibrium Dissociation Constant, K / 76
4.2 The Kinetic Approach to Equilibrium / 78
4.3 Binding Measurements at Equilibrium / 80
4.4 Graphic Analysis of Equilibrium Ligand Binding Data / 88
4.5 Equilibrium Binding with Ligand Depletion (Tight Binding
Interactions) / 94
4.6 Competition Among Ligands for a Common Binding Site / 95
4.7 Experimental Methods for Measuring Ligand Binding / 96
4.8 Summary / 107
References and Further Reading / 108
5 Kinetics of Single-Substrate Enzyme Reactions 109
5.1 The Time Course of Enzymatic Reactions / 109
5.2 Effects of Substrate Concentration on Velocity / 111
5.3 The Rapid Equilibrium Model of Enzyme Kinetics / 113
5.4 The Steady State Model of Enzyme Kinetics / 115
5.5 The Significance of k and K / 120
5.6 Experimental Measurement of k and K / 124
5.7 Other Linear Transformations of Enzyme Kinetic Data / 133
5.8 Measurements at Low Substrate Concentrations / 136
5.9 Deviations from Hyperbolic Kinetics / 137
5.10 Transient State Kinetic Measurements / 141
5.11 Summary / 145
References and Further Reading / 145
6 Chemical Mechanisms in Enzyme Catalysis 146
6.1 Substrate—Active Site Complementarity / 147
6.2 Rate Enhancement Through Transition State Stabilization / 151
6.3 Chemical Mechanisms for Transition State Stabilization / 154
6.4 The Serine Proteases: An Illustrative Example / 178
6.5 Enzymatic Reaction Nomenclature / 184
viii CONTENTS
6.6 Summary / 186
References and Further Reading / 186
7 Experimental Measures of Enzyme Activity 188
7.1 Initial Velocity Measurements / 188
7.2 Detection Methods / 204
7.3 Separation Methods in Enzyme Assays / 223
7.4 Factors Affecting the Velocity of Enzymatic Reactions / 238
7.5 Reporting Enzyme Activity Data / 257
7.6 Enzyme Stability / 258
7.7 Summary / 263
References and Further Reading / 263
8 Reversible Inhibitors 266
8.1 Equilibrium Treatment of Reversible Inhibition / 268
8.2 Modes of Reversible Inhibition / 270
8.3 Graphic Determination of Inhibitor Type / 273
8.4 Dose—Response Curves of Enzyme Inhibition / 282
8.5 Mutually Exclusive Binding of Two Inhibitors / 287
8.6 Structure—Activity Relationships and Inhibitor Design / 291
8.6 Summary / 303
References and Further Reading / 303
9 Tight Binding Inhibitors 305
9.1 Identifying Tight Binding Inhibition / 305
9.2 Distinguishing Inhibitor Type for Tight Binding Inhibitors / 307
9.3 Determining K for Tight Binding Inhibitors / 310
9.4 Use of Tight Binding Inhibitors to Determine Active Enzyme
Concentration / 313
9.5 Summary / 315
References and Further Reading / 316
10 Time-Dependent Inhibition 318
10.1 Progress Curves for Slow Binding Inhibitors / 321
10.2 Distinguishing Between Slow Binding Schemes / 325
10.3 Distinguishing Between Modes of Inhibitor Interaction with
Enzyme / 330
CONTENTS ix
10.4 Determining Reversibility / 332
10.5 Examples of Slow Binding Enzyme Inhibitors / 334
10.6 Summary / 348
References and Further Reading / 349
11 Enzyme Reactions with Multiple Substrates 350
11.1 Reaction Nomenclature / 350
11.2 Bi Bi Reaction Mechanisms / 352
11.3 Distinguishing Between Random and Compulsory Ordered
Mechanisms by Inhibition Pattern / 357
11.4 Isotope Exchange Studies for Distinguishing Reaction
Mechanisms / 360
11.5 Using the King—Altman Method to Determine Velocity
Equations / 362
11.6 Summary / 364
References and Further Reading / 366
12 Cooperativity in Enzyme Catalysis 367
12.1 Historic Examples of Cooperativity and Allostery in Proteins / 368
12.2 Models of Allosteric Behavior / 373
12.3 Effects of Cooperativity on Velocity Curves / 379
12.4 Sigmoidal Kinetics for Nonallosteric Enzymes / 382
12.5 Summary / 383
References and Further Reading / 384
Appendix I. Suppliers of Reagents and Equipment for
Enzyme Studies 385
Appendix II. Useful Computer Software and Web Sites
for Enzyme Studies 387
Index 391
2.格式：PDF
3.作者：Robert A. Copeland
4.大小：6MB
5.出版社：2000 by Wiley-VCH, Inc.
7.简介：见下
本书经我在本论坛里没有找到有上传的，与大家共享。原先在FTP资源区，经老赵提醒放在专业区，由于好几位战友PM我要这本书，现重新在专业区申请！
下载目录在 /基础医学区/蛋白质技术专业组/pub/
1 A Brief History of Enzymology 1
1.1 Enzymes in Antiquity / 2
1.2 Early Enzymology / 3
1.3 The Development of Mechanistic Enzymology / 4
1.4 Studies of Enzyme Structure / 5
1.5 Enzymology Today / 7
1.6 Summary / 8
References and Further Reading / 10
2 Chemical Bonds and Reactions in Biochemistry 11
2.1 Atomic and Molecular Orbitals / 11
2.2 Thermodynamics of Chemical Reactions / 23
2.3 Acid—Base Chemistry / 29
2.4 Noncovalent Interactions in Reversible Binding / 32
2.5 Rates of Chemical Reactions / 35
2.6 Summary / 41
References and Further Reading / 41
3 Structural Components of Enzymes 42
3.1 The Amino Acids / 42
3.2 The Peptide Bond / 53
3.3 Amino Acid Sequence or Primary Structure / 55
3.4 Secondary Structure / 57
3.5 Tertiary Structure / 62
vii
3.6 Subunits and Quaternary Structure / 65
3.7 Cofactors in Enzymes / 68
3.8 Summary / 71
References and Further Reading / 74
4 Protein‒Ligand Binding Equilibria 76
4.1 The Equilibrium Dissociation Constant, K / 76
4.2 The Kinetic Approach to Equilibrium / 78
4.3 Binding Measurements at Equilibrium / 80
4.4 Graphic Analysis of Equilibrium Ligand Binding Data / 88
4.5 Equilibrium Binding with Ligand Depletion (Tight Binding
Interactions) / 94
4.6 Competition Among Ligands for a Common Binding Site / 95
4.7 Experimental Methods for Measuring Ligand Binding / 96
4.8 Summary / 107
References and Further Reading / 108
5 Kinetics of Single-Substrate Enzyme Reactions 109
5.1 The Time Course of Enzymatic Reactions / 109
5.2 Effects of Substrate Concentration on Velocity / 111
5.3 The Rapid Equilibrium Model of Enzyme Kinetics / 113
5.4 The Steady State Model of Enzyme Kinetics / 115
5.5 The Significance of k and K / 120
5.6 Experimental Measurement of k and K / 124
5.7 Other Linear Transformations of Enzyme Kinetic Data / 133
5.8 Measurements at Low Substrate Concentrations / 136
5.9 Deviations from Hyperbolic Kinetics / 137
5.10 Transient State Kinetic Measurements / 141
5.11 Summary / 145
References and Further Reading / 145
6 Chemical Mechanisms in Enzyme Catalysis 146
6.1 Substrate—Active Site Complementarity / 147
6.2 Rate Enhancement Through Transition State Stabilization / 151
6.3 Chemical Mechanisms for Transition State Stabilization / 154
6.4 The Serine Proteases: An Illustrative Example / 178
6.5 Enzymatic Reaction Nomenclature / 184
viii CONTENTS
6.6 Summary / 186
References and Further Reading / 186
7 Experimental Measures of Enzyme Activity 188
7.1 Initial Velocity Measurements / 188
7.2 Detection Methods / 204
7.3 Separation Methods in Enzyme Assays / 223
7.4 Factors Affecting the Velocity of Enzymatic Reactions / 238
7.5 Reporting Enzyme Activity Data / 257
7.6 Enzyme Stability / 258
7.7 Summary / 263
References and Further Reading / 263
8 Reversible Inhibitors 266
8.1 Equilibrium Treatment of Reversible Inhibition / 268
8.2 Modes of Reversible Inhibition / 270
8.3 Graphic Determination of Inhibitor Type / 273
8.4 Dose—Response Curves of Enzyme Inhibition / 282
8.5 Mutually Exclusive Binding of Two Inhibitors / 287
8.6 Structure—Activity Relationships and Inhibitor Design / 291
8.6 Summary / 303
References and Further Reading / 303
9 Tight Binding Inhibitors 305
9.1 Identifying Tight Binding Inhibition / 305
9.2 Distinguishing Inhibitor Type for Tight Binding Inhibitors / 307
9.3 Determining K for Tight Binding Inhibitors / 310
9.4 Use of Tight Binding Inhibitors to Determine Active Enzyme
Concentration / 313
9.5 Summary / 315
References and Further Reading / 316
10 Time-Dependent Inhibition 318
10.1 Progress Curves for Slow Binding Inhibitors / 321
10.2 Distinguishing Between Slow Binding Schemes / 325
10.3 Distinguishing Between Modes of Inhibitor Interaction with
Enzyme / 330
CONTENTS ix
10.4 Determining Reversibility / 332
10.5 Examples of Slow Binding Enzyme Inhibitors / 334
10.6 Summary / 348
References and Further Reading / 349
11 Enzyme Reactions with Multiple Substrates 350
11.1 Reaction Nomenclature / 350
11.2 Bi Bi Reaction Mechanisms / 352
11.3 Distinguishing Between Random and Compulsory Ordered
Mechanisms by Inhibition Pattern / 357
11.4 Isotope Exchange Studies for Distinguishing Reaction
Mechanisms / 360
11.5 Using the King—Altman Method to Determine Velocity
Equations / 362
11.6 Summary / 364
References and Further Reading / 366
12 Cooperativity in Enzyme Catalysis 367
12.1 Historic Examples of Cooperativity and Allostery in Proteins / 368
12.2 Models of Allosteric Behavior / 373
12.3 Effects of Cooperativity on Velocity Curves / 379
12.4 Sigmoidal Kinetics for Nonallosteric Enzymes / 382
12.5 Summary / 383
References and Further Reading / 384
Appendix I. Suppliers of Reagents and Equipment for
Enzyme Studies 385
Appendix II. Useful Computer Software and Web Sites
for Enzyme Studies 387
Index 391
