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        [下载]由wiley公司出版的酶学(Enzymes)第二版

        丁香园论坛

        1603
        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
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