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Enzymes : a practical introduction to structure, mechanism, and data analysis / / Robert Allen Copeland
Enzymes : a practical introduction to structure, mechanism, and data analysis / / Robert Allen Copeland
Autore Copeland Robert Allen
Edizione [Third edition.]
Pubbl/distr/stampa Hoboken, New Jersey : , : Wiley, , 2023
Descrizione fisica 1 online resource (579 pages)
Disciplina 572.7
Soggetto topico Enzymes
Enzymology
ISBN 1-119-79330-0
1-119-79328-9
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Cover -- Title Page -- Copyright -- Contents -- PREFACE TO THE THIRD EDITION -- PREFACE TO THE SECONDEDITION -- PREFACE TO THE FIRST EDITION -- ACKNOWLEDGMENTS -- Chapter 1 A BRIEF HISTORY OF ENZYMOLOGY -- 1.1 ENZYMES IN ANTIQUITY -- 1.2 EARLY ENZYMOLOGY -- 1.3 THE DEVELOPMENT OF MECHANISTIC ENZYMOLOGY -- 1.4 STUDIES OF ENZYME STRUCTURE -- 1.5 ENZYMOLOGY TODAY -- 1.6 SUMMARY -- 1.7 REFERENCES AND FURTHER READING -- Chapter 2 Chemical Bonds and Reactions in Biochemistry -- 2.1 Atomic and Molecular Orbitals -- 2.1.1 Atomic Orbitals -- 2.1.2 Molecular Orbitals -- 2.1.3 Hybrid Orbitals -- 2.1.4 Resonance and Aromaticity -- 2.1.5 Different Electronic Configurations Have Different Potential Energies -- 2.2 Thermodynamics of Chemical Reactions -- 2.2.1 The Transition State of Chemical Reactions -- 2.3 Acid-base Chemistry -- 2.4 Noncovalent Interactions in Reversible Binding -- 2.4.1 Electrostatic Interactions -- 2.4.2 Hydrogen Bonding -- 2.4.3 Hydrophobic Interactions -- 2.4.4 Van der Waals Forces -- 2.5 Rates of Chemical Reactions -- 2.5.1 Reaction Order -- 2.5.2 Reversible Chemical Reactions -- 2.5.3 Measurement of Initial Velocity -- 2.6 Summary -- 2.7 References and Further Reading -- Chapter 3 Structural Components of Enzymes -- 3.1 THE AMINO ACIDS -- 3.1.1 Properties of Amino‐Acid Side Chains -- 3.1.1.1 Hydrophobicity -- 3.1.1.2 Hydrogen Bonding -- 3.1.1.3 Salt‐Bridge Formation -- 3.1.2 Amino Acids as Acids and Bases -- 3.1.3 Cation and Metal Binding -- 3.1.4 Anion and Polyanion Binding -- 3.1.5 Covalent Bond Formation -- 3.1.5.1 Disulfide Bonds -- 3.1.5.2 Phosphorylation -- 3.1.5.3 Glycosylation -- 3.1.6 Steric Bulk -- 3.2 THE PEPTIDE BOND -- 3.3 AMINO ACID SEQUENCE OR PRIMARY STRUCTURE -- 3.4 SECONDARY STRUCTURE -- 3.4.1 The Right‐Handed & -- bfitalpha -- Helix -- 3.4.2 The & -- bfitbeta -- ‐Pleated Sheet -- 3.4.3 & -- bfitbeta.
Turns -- 3.4.4 Other Secondary Structures -- 3.4.5 Supersecondary Structures -- 3.5 TERTIARY STRUCTURE -- 3.5.1 Domains -- 3.6 SUBUNITS AND QUATERNARY STRUCTURE -- 3.7 COFACTORS IN ENZYMES -- 3.8 CONFORMATIONAL DYNAMICS AND ENZYME FUNCTION -- 3.9 METHODS OF PROTEIN STRUCTURE DETERMINATION -- 3.9.1 X‐ray Crystallography -- 3.9.2 NMR Spectroscopy -- 3.9.3 Cryo‐Electron Microscopy (Cryo‐EM) -- 3.10 SUMMARY -- 3.11 REFERENCES AND FURTHER READING -- Chapter 4 PROTEIN-LIGAND BINDING EQUILIBRIA -- 4.1 THE EQUILIBRIUM DISSOCIATION CONSTANT, K -- 4.2 THE KINETIC APPROACH TO EQUILIBRIUM -- 4.3 BINDING MEASUREMENTS AT EQUILIBRIUM -- 4.3.1 Derivation of the Langmuir Isotherm -- 4.3.2 Multiple Binding Sites -- 4.3.2.1 Multiple Equivalent Binding Sites -- 4.3.2.2 Multiple Nonequivalent Binding Sites -- 4.3.2.3 Cooperative Interactions Among Multiple Binding Sites -- 4.3.3 Correction for Nonspecific Binding -- 4.4 GRAPHIC ANALYSIS OF EQUILIBRIUM LIGAND‐BINDING DATA -- 4.4.1 Direct Plots on Semilog Scale -- 4.4.2 Linear Transformations of Binding Data: The Wolff Plots -- 4.5 EQUILIBRIUM BINDING WITH LIGAND DEPLETION (TIGHT BINDING INTERACTIONS) -- 4.6 COMPETITION AMONG LIGANDS FOR A COMMON BINDING SITE -- 4.7 PROTEIN DYNAMICS IN RECEPTOR-LIGAND BINDING -- 4.8 ORTHOSTERIC AND ALLOSTERIC LIGAND BINDING SITES -- 4.9 EXPERIMENTAL METHODS FOR MEASURING LIGAND BINDING -- 4.9.1 Methods Based on Mass or Mobility Differences -- 4.9.1.1 Equilibrium Dialysis -- 4.9.1.2 Membrane Filtration Methods -- 4.9.1.3 Size Exclusion Chromatography -- 4.9.1.4 Microscale Thermophoresis -- 4.9.2 Spectroscopic Methods -- 4.9.2.1 Fluorescence Spectroscopy -- 4.9.2.2 Surface Plasmon Resonance -- 4.9.3 Ligand‐Induced Protein Stabilization -- 4.9.3.1 Thermal Denaturation of Proteins -- 4.9.3.2 Chemical Denaturation of Proteins -- 4.10 SUMMARY -- 4.11 REFERENCES AND FURTHER READING.
Chapter 5 STEADY‐STATE KINETICS OF SINGLE‐SUBSTRATE ENZYME REACTIONS -- 5.1 THE TIME COURSE OF ENZYMATIC REACTIONS -- 5.2 EFFECTS OF SUBSTRATE CONCENTRATION ON VELOCITY -- 5.3 THE RAPID EQUILIBRIUM MODEL OF ENZYME KINETICS -- 5.4 THE STEADY‐STATE MODEL OF ENZYME KINETICS -- 5.5 THE SIGNIFICANCE OF AND K -- 5.5.1 Km -- 5.5.2 kcat -- 5.5.3 kcat/Km -- 5.5.4 Diffusion‐Controlled Reactions and Kinetic Perfection -- 5.6 EXPERIMENTAL MEASUREMENT OF AND K -- 5.6.1 Graphical Determinations from Untransformed Data -- 5.6.2 Lineweaver-Burk Plots of Enzyme Kinetics -- 5.7 OTHER LINEAR TRANSFORMATIONS OF ENZYME KINETIC DATA -- 5.7.1 Eadie-Hofstee Plots -- 5.7.2 Hanes-Wolff Plots -- 5.7.3 Eisenthal-Cornish‐Bowden Direct Plots -- 5.8 MEASUREMENTS AT LOW SUBSTRATE CONCENTRATIONS -- 5.9 DEVIATIONS FROM HYPERBOLIC KINETICS -- 5.10 SUMMARY -- 5.11 REFERENCES AND FURTHER READING -- Chapter 6 CHEMICAL MECHANISMS IN ENZYME CATALYSIS -- 6.1 Substrate-Active Site Complementarity -- 6.2 RATE ENHANCEMENT THROUGH TRANSITION STATE STABILIZATION -- 6.3 CHEMICAL MECHANISMS FOR TRANSITION STATE STABILIZATION -- 6.3.1 Approximation of Reactants -- 6.3.2 Covalent Catalysis -- 6.3.2.1 Nucleophilic Catalysis -- 6.3.2.2 Electrophilic Catalysis -- 6.3.3 General Acid/Base Catalysis -- 6.3.4 Conformational Distortion -- 6.3.5 Preorganized Active Site Complementarity to the Transition State -- 6.4 THE SERINE PROTEASES: AN ILLUSTRATIVE EXAMPLE -- 6.5 ENZYMATIC REACTION NOMENCLATURE -- 6.6 SUMMARY -- 6.7 REFERENCES AND FURTHER READING -- Chapter 7 EXPERIMENTAL MEASURES OF STEADY‐STATE ENZYME ACTIVITY -- 7.1 INITIAL VELOCITY MEASUREMENTS -- 7.1.1 Direct, Indirect, and Coupled Assays -- 7.1.2 Analysis of Progress Curves: Measuring True Steady‐State Velocity -- 7.1.3 Continuous Versus End Point Assays -- 7.1.4 Initiating, Mixing, and Stopping Reactions.
7.1.5 The Importance of Running Controls -- 7.2 DETECTION METHODS -- 7.2.1 Assays Based on Optical Spectroscopy -- 7.2.2 Absorption Measurements -- 7.2.3 Choosing an Analytical Wavelength -- 7.2.4 Optical Cells -- 7.2.5 Errors in Absorption Spectroscopy -- 7.2.6 Fluorescence Measurements -- 7.2.7 Internal Fluorescence Quenching and Energy Transfer -- 7.2.8 Errors in Fluorescence Measurements -- 7.2.9 Radioisotopic Measurements -- 7.2.10 Errors in Radioactivity Measurements -- 7.2.11 Other Detection Methods -- 7.3 SEPARATION METHODS IN ENZYME ASSAYS -- 7.3.1 Separation of Proteins from Low Molecular Weight Solutes -- 7.3.2 Chromatographic Separation Methods -- 7.3.3 Electrophoretic Methods in Enzyme Assays -- 7.4 FACTORS AFFECTING THE VELOCITY OF ENZYMATIC REACTIONS -- 7.4.1 Enzyme Concentration -- 7.4.2 pH Effects -- 7.4.3 Temperature Effects -- 7.4.4 Viscosity Effects -- 7.4.5 Isotope Effects in Enzyme Kinetics -- 7.5 REPORTING ENZYME ACTIVITY DATA -- 7.6 ENZYME STABILITY -- 7.6.1 Stabilizing Enzymes During Storage -- 7.6.2 Enzyme Inactivation During Activity Assays -- 7.7 SUMMARY -- 7.8 REFERENCES AND FURTHER READING -- Chapter 8 TRANSIENT‐STATE KINETICS -- 8.1 TIMESCALE OF PRE‐STEADY‐STATE TURNOVER -- 8.2 INSTRUMENTATION FOR TRANSIENT KINETIC MEASUREMENTS -- 8.3 ESTIMATING INITIAL CONDITIONS FOR TRANSIENT KINETIC MEASUREMENTS -- 8.4 EXAMPLES OF SOME COMMON TRANSIENT KINETIC REACTION MECHANISMS -- 8.4.1 One Step, Irreversible Binding -- 8.4.2 One Step, Reversible Binding -- 8.4.3 Consecutive, Irreversible Reaction -- 8.4.4 Consecutive, Reversible Reaction with a Fast First Step (Pre‐equilibrium Reaction) -- 8.4.5 Consecutive, Reversible Reaction with a Fast Second Step (Enzyme Pre‐isomerization) -- 8.5 EXAMPLES OF TRANSIENT KINETIC STUDIES FROM THE LITERATURE -- 8.5.1 Study of Substrate and Inhibitor Interactions with the Alzheimer's Disease &.
rmbeta -- ‐Site Amyloid Precursor Protein‐Cleaving Enzyme (BACE) -- 8.5.2 Study of the Mechanism of Time‐Dependent Inhibition of Staphylococcus aureus Polypeptide Deformylase -- 8.6 SUMMARY -- 8.7 REFERENCES AND FURTHER READING -- Chapter 9 ENZYME REGULATION -- 9.1 Active and Inactive Conformational States -- 9.2 Post‐Translational Modifications -- 9.2.1 Proteolytic Processing -- 9.2.2 Covalent Modification of Amino Acid Side Chains -- 9.3 Enzyme Regulation Through Protein-Protein Interactions -- 9.4 Small‐Molecule Allosteric Ligands -- 9.4.1 Homotropic and Heterotropic Allostery -- 9.4.2 Intramolecular and Intermolecular Allostery -- 9.5 Quantitative Measurements of Enzyme Activation and Inhibition -- 9.5.1 Thermodynamic Measurement of Activator-Enzyme Interactions -- 9.5.2 Kinetic Measurement of Enzyme Activation by PTM -- 9.6 Regulation of Protein Kinases -- 9.6.1 Kinase Activation by PTM -- 9.6.2 Kinase Regulation by Protein Association -- 9.6.3 Kinase Activation by Oligomerization -- 9.6.4 Kinase Regulation by Small‐Molecule Binding -- 9.6.5 Small‐Molecule Mimicry of Intramolecular Allostery -- 9.7 Summary -- 9.8 References and Further Reading -- Chapter 10 REVERSIBLE INHIBITORS -- 10.1 EQUILIBRIUM TREATMENT OF REVERSIBLE INHIBITION -- 10.2 THERMODYNAMIC MODES OF REVERSIBLE INHIBITION -- 10.2.1 Pure Competitive Inhibition, Exclusive Binding to Free Enzyme (E): α & -- equals -- ∞ -- 10.2.2 Mixed or Noncompetitive Inhibition -- 10.2.2.1 Mixed Inhibitors That Bind Preferentially to the Free Enzyme (E): α > -- 1 -- 10.2.2.2 Mixed Inhibitors That Bind Equipotently to E and ES: α & -- equals -- 1 -- 10.2.2.3 Mixed Inhibitors That Bind Preferentially to the Enzyme-Substrate Complex (ES): α < -- 1 -- 10.2.3 Pure Uncompetitive Inhibitors, Exclusive Binding to the Enzyme‐Substrate Complex (ES): α ≪ 1 -- 10.2.4 Partial Inhibitors.
10.3 EFFECTS OF INHIBITORS ON STEADY‐STATE PARAMETERS.
Record Nr. UNINA-9910677826003321
Copeland Robert Allen  
Hoboken, New Jersey : , : Wiley, , 2023
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Enzymes [[electronic resource] ] : a practical introduction to structure, mechanism, and data analysis / / Robert A. Copeland
Enzymes [[electronic resource] ] : a practical introduction to structure, mechanism, and data analysis / / Robert A. Copeland
Autore Copeland Robert Allen
Edizione [2nd ed.]
Pubbl/distr/stampa New York, : J. Wiley, c2014
Descrizione fisica 1 online resource (417 p.)
Disciplina 572.7
Soggetto topico Enzymes
Enzymology
ISBN 1-280-36703-2
9786610367030
0-470-23916-6
0-471-46185-7
0-471-22063-9
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto ENZYMES SECOND EDITION; CONTENTS; Preface; Acknowledgments; Preface to the First Edition; 1 A Brief History of Enzymology; 1.1 Enzymes in Antiquity; 1.2 Early Enzymology; 1.3 The Development of Mechanistic Enzymology; 1.4 Studies of Enzyme Structure; 1.5 Enzymology Today; 1.6 Summary; References and Further Reading; 2 Chemical Bonds and Reactions in Biochemistry; 2.1 Atomic and Molecular Orbitals; 2.2 Thermodynamics of Chemical Reactions; 2.3 Acid-Base Chemistry; 2.4 Noncovalent Interactions in Reversible Binding; 2.5 Rates of Chemical Reactions; 2.6 Summary; References and Further Reading
3 Structural Components of Enzymes3.1 The Amino Acids; 3.2 The Peptide Bond; 3.3 Amino Acid Sequence or Primary Structure; 3.4 Secondary Structure; 3.5 Tertiary Structure; 3.6 Subunits and Quaternary Structure; 3.7 Cofactors in Enzymes; 3.8 Summary; References and Further Reading; 4 Protein-Ligand Binding Equilibria; 4.1 The Equilibrium Dissociation Constant, K(d); 4.2 The Kinetic Approach to Equilibrium; 4.3 Binding Measurements at Equilibrium; 4.4 Graphic Analysis of Equilibrium Ligand Binding Data; 4.5 Equilibrium Binding with Ligand Depletion (Tight Binding Interactions)
4.6 Competition Among Ligands for a Common Binding Site4.7 Experimental Methods for Measuring Ligand Binding; 4.8 Summary; References and Further Reading; 5 Kinetics of Single-Substrate Enzyme Reactions; 5.1 The Time Course of Enzymatic Reactions; 5.2 Effects of Substrate Concentration on Velocity; 5.3 The Rapid Equilibrium Model of Enzyme Kinetics; 5.4 The Steady State Model of Enzyme Kinetics; 5.5 The Significance of k(cat) and K(m); 5.6 Experimental Measurement of k(cat) and K(m); 5.7 Other Linear Transformations of Enzyme Kinetic Data; 5.8 Measurements at Low Substrate Concentrations
5.9 Deviations from Hyperbolic Kinetics5.10 Transient State Kinetic Measurements; 5.11 Summary; References and Further Reading; 6 Chemical Mechanisms in Enzyme Catalysis; 6.1 Substrate-Active Site Complementarity; 6.2 Rate Enhancement Through Transition State Stabilization; 6.3 Chemical Mechanisms for Transition State Stabilization; 6.4 The Serine Proteases: An Illustrative Example; 6.5 Enzymatic Reaction Nomenclature; 6.6 Summary; References and Further Reading; 7 Experimental Measures of Enzyme Activity; 7.1 Initial Velocity Measurements; 7.2 Detection Methods
7.3 Separation Methods in Enzyme Assays7.4 Factors Affecting the Velocity of Enzymatic Reactions; 7.5 Reporting Enzyme Activity Data; 7.6 Enzyme Stability; 7.7 Summary; References and Further Reading; 8 Reversible Inhibitors; 8.1 Equilibrium Treatment of Reversible Inhibition; 8.2 Modes of Reversible Inhibition; 8.3 Graphic Determination of Inhibitor Type; 8.4 Dose-Response Curves of Enzyme Inhibition; 8.5 Mutually Exclusive Binding of Two Inhibitors; 8.6 Structure-Activity Relationships and Inhibitor Design; 8.7 Summary; References and Further Reading; 9 Tight Binding Inhibitors
9.1 Identifying Tight Binding Inhibition
Record Nr. UNINA-9910142503503321
Copeland Robert Allen  
New York, : J. Wiley, c2014
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Enzymes [[electronic resource] ] : a practical introduction to structure, mechanism, and data analysis / / Robert A. Copeland
Enzymes [[electronic resource] ] : a practical introduction to structure, mechanism, and data analysis / / Robert A. Copeland
Autore Copeland Robert Allen
Edizione [2nd ed.]
Pubbl/distr/stampa New York, : J. Wiley, c2014
Descrizione fisica 1 online resource (417 p.)
Disciplina 572.7
Soggetto topico Enzymes
Enzymology
ISBN 1-280-36703-2
9786610367030
0-470-23916-6
0-471-46185-7
0-471-22063-9
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto ENZYMES SECOND EDITION; CONTENTS; Preface; Acknowledgments; Preface to the First Edition; 1 A Brief History of Enzymology; 1.1 Enzymes in Antiquity; 1.2 Early Enzymology; 1.3 The Development of Mechanistic Enzymology; 1.4 Studies of Enzyme Structure; 1.5 Enzymology Today; 1.6 Summary; References and Further Reading; 2 Chemical Bonds and Reactions in Biochemistry; 2.1 Atomic and Molecular Orbitals; 2.2 Thermodynamics of Chemical Reactions; 2.3 Acid-Base Chemistry; 2.4 Noncovalent Interactions in Reversible Binding; 2.5 Rates of Chemical Reactions; 2.6 Summary; References and Further Reading
3 Structural Components of Enzymes3.1 The Amino Acids; 3.2 The Peptide Bond; 3.3 Amino Acid Sequence or Primary Structure; 3.4 Secondary Structure; 3.5 Tertiary Structure; 3.6 Subunits and Quaternary Structure; 3.7 Cofactors in Enzymes; 3.8 Summary; References and Further Reading; 4 Protein-Ligand Binding Equilibria; 4.1 The Equilibrium Dissociation Constant, K(d); 4.2 The Kinetic Approach to Equilibrium; 4.3 Binding Measurements at Equilibrium; 4.4 Graphic Analysis of Equilibrium Ligand Binding Data; 4.5 Equilibrium Binding with Ligand Depletion (Tight Binding Interactions)
4.6 Competition Among Ligands for a Common Binding Site4.7 Experimental Methods for Measuring Ligand Binding; 4.8 Summary; References and Further Reading; 5 Kinetics of Single-Substrate Enzyme Reactions; 5.1 The Time Course of Enzymatic Reactions; 5.2 Effects of Substrate Concentration on Velocity; 5.3 The Rapid Equilibrium Model of Enzyme Kinetics; 5.4 The Steady State Model of Enzyme Kinetics; 5.5 The Significance of k(cat) and K(m); 5.6 Experimental Measurement of k(cat) and K(m); 5.7 Other Linear Transformations of Enzyme Kinetic Data; 5.8 Measurements at Low Substrate Concentrations
5.9 Deviations from Hyperbolic Kinetics5.10 Transient State Kinetic Measurements; 5.11 Summary; References and Further Reading; 6 Chemical Mechanisms in Enzyme Catalysis; 6.1 Substrate-Active Site Complementarity; 6.2 Rate Enhancement Through Transition State Stabilization; 6.3 Chemical Mechanisms for Transition State Stabilization; 6.4 The Serine Proteases: An Illustrative Example; 6.5 Enzymatic Reaction Nomenclature; 6.6 Summary; References and Further Reading; 7 Experimental Measures of Enzyme Activity; 7.1 Initial Velocity Measurements; 7.2 Detection Methods
7.3 Separation Methods in Enzyme Assays7.4 Factors Affecting the Velocity of Enzymatic Reactions; 7.5 Reporting Enzyme Activity Data; 7.6 Enzyme Stability; 7.7 Summary; References and Further Reading; 8 Reversible Inhibitors; 8.1 Equilibrium Treatment of Reversible Inhibition; 8.2 Modes of Reversible Inhibition; 8.3 Graphic Determination of Inhibitor Type; 8.4 Dose-Response Curves of Enzyme Inhibition; 8.5 Mutually Exclusive Binding of Two Inhibitors; 8.6 Structure-Activity Relationships and Inhibitor Design; 8.7 Summary; References and Further Reading; 9 Tight Binding Inhibitors
9.1 Identifying Tight Binding Inhibition
Record Nr. UNINA-9910677846903321
Copeland Robert Allen  
New York, : J. Wiley, c2014
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / by Robert A. Copeland
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / by Robert A. Copeland
Autore Copeland Robert Allen
Edizione [2nd ed.]
Pubbl/distr/stampa Hoboken, N.J., : Wiley, c2013
Descrizione fisica 1 online resource (572 p.)
Disciplina 615/.19
Soggetto topico Enzyme inhibitors - Therapeutic use - Testing
Drugs - Design
Enzyme inhibitors - Structure-activity relationships
ISBN 1-118-54039-5
1-299-24215-4
1-118-54040-9
1-118-54028-X
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Machine generated contents note: Foreword.Preface.Acknowledgments.1. Why Enzymes as Drug Targets?1.1 Enzymes Are Essentials for Life.1.2 Enzyme Structure and Catalysis.1.3 Permutations of Enzyme Structure During Catalysis.1.4 Other Reasons for Studying Enzymes.1.5 Summary.References.2. Enzyme Reaction Mechanisms.2.1 Initial Binding of Substrate.2.2 Noncovalent Forces in Reversible Ligand Binding to Enzymes.2.2.1 Electrostatic Forces.2.2.2 Hydrogen Bonds.2.2.3 Hydrophobic Forces.2.2.4 van der Waals Forces.2.3 Transformations of the Bond Substrate.2.3.1 Strategies for Transition State Stabilization.2.3.2 Enzyme Active Sites Are Most Complementary to the Transition State Structure.2.4 Steady State Analysis of Enzyme Kinetics.2.4.1 Factors Affecting the Steady State Kinetic Constants.2.5 Graphical Determination of kcat and KM2.6 Reactions Involving Multiple Substates.2.6.1 Bisubstrate Reaction Mechanisms.2.7 Summary.References.3. Reversible Modes of Inhibitor Interactions with Enzymes.3.1 Enzyme-Inhibitor Binding Equilibria.3.2 Competitive Inhibition.3.3 Noncompetitive Inhibition.3.3.1 Mutual Exclusively Studies.3.4 Uncompetitive Inhibition.3.5 Inhibition Modality in Bisubstrate Reactions.3.6 Value of Knowing Inhibitor Modality.3.6.1 Quantitative Comparisons of Inhibitor Affinity.3.6.2 Relating Ki to Binding Energy.3.6.3 Defining Target Selectivity by Ki Values.3.6.4 Potential Advantages and Disadvantages of Different Inhibition Modalities In Vivo.3.6.5 Knowing Inhibition Modality Is Important for Structure-Based Lead Organization.3.7 Summary.References.4. Assay Considerations for Compound Library Screening.4.1 Defining Inhibition Signal Robustness, and Hit Criteria.4.2 Measuring Initial Velocity.4.2.1 End-Point and Kinetic Readouts.4.2.2 Effects of Enzyme Concentration.4.3 Balanced Assay Conditions.4.3.1 Balancing Conditions for Multisubstrate Reactions.4.4 Order of Reagent Addition.4.5 Use of Natural Substrates and Enzymes.4.6 Coupled Enzyme Assays.4.7 Hit Validation and Progression.4.8 Summary.References.5. Lead Optimization and Structure-Activity Relationships for Reversible Inhibitors.5.1 Concentration-Response Plots and IC50 Determination.5.1.1 The Hill Coefficient.5.1.2 Graphing and Reporting Concentration-Response Data.5.2 Testing for Reversibility.5.3 Determining Reversible Inhibition Modality and Dissociation Constant.5.4 Comparing Relative Affinity.5.4.1 Compound Selectivity.5.5 Associating Cellular Effects with Target Enzyme Inhibition.5.5.1 Cellular Phenotype Should Be Consistent with Genetic Knockout or Knockdown of the Target Enzyme.5.5.2 Cellular Activity Should Require a Certain Affinity for the target Enzyme.5.5.3 Buildup of Substrate and/or Diminution of Product for the Target Enzyme Should Be Observed in Cells.5.5.4 Cellular Phenotype Should Be Reversed by Cell-Permeable Product or Downstream Metabolites of the Target Enzyme Activity.5.5.5 Mutation of the Target Enzyme Should Lead to Resistance or Hypersensitivity to Inhibitors.5.6 Summary.References.6. Slow Binding Inhibitors.6.1 Determining kobs: The Rate Constant for Onset of Inhibition.6.2 Mechanisms of Slow Binding Inhibition.6.3 Determination of Mechanism and Assessment of True Affinity.6.3.1 Potential Clinical Advantages of Slow Off-rate Inhibitors.6.4 Determining Inhibition Modality for Slow Binding Inhibitors.6.5 SAR for Slow Binding Inhibitors.6.6 Some Examples of Pharmacologically Interesting Slow Binding Inhibitors.6.6.1 Examples of Scheme B: Inhibitors of Zinc Peptidases and Proteases.6.6.2 Example of Scheme C: Inhibition of Dihydrofolate Reductase by Methotresate.6.6.3 Example of Scheme C: Inhibition of Calcineurin by FKBP-Inhibitor Complexes.6.6.4 Example of Scheme C When Ki* << Ki: Aspartyl Protease Inhibitors.6.6.5 Example of Scheme C When k6 Is Very Small: Selective COX2 Inhibitors.6.7 Summary.References.7. Tight Binding Inhibitors.7.1 Effects of Tight Binding Inhibition Concentration-Response Data.7.2 The IC50 Value Depends on Kiapp and [E]T.7.3 Morrison's Quadratic Equation for Fiting Concentration-Response Data for Tight Binding Inhibitors.7.3.1 Optimizing Conditions for Kiapp Determination Using Morrison's Equation.7.3.2 Limits on Kiapp Determinations.7.3.3 Use of a Cubic Equation When Both Substrate and Inhibitor Are Tight Binding.7.4 Determining Modality for Tight Binding Enzyme Inhibitors.7.5 Tight Binding Inhibitors Often Display Slow Binding Behavior.7.6 Practical Approaches to Overcoming the Tight Binding Limit in Determine Ki.7.7 Enzyme-Reaction Intermediate Analogues as Example of Tight Binding Inhibitors.7.7.1 Bisubstrate Analogues.7.7.2 Testing for Transition State Mimicry.7.8 Potential Clinical Advantages of Tight Binding Inhibitors.7.9 Determination of [E]T Using Tight Binding Inhibitors.7.10 Summary.References.8. Irreversible Enzyme Inactivators.8.1 Kinetic Evaluation of Irreversible Enzyme Inactivators.8.2 Affinity Labels.8.2.1 Quiescent Affinity Labels.8.2.2 Potential Liabilities of Affinity Labels as Drugs.8.3 Mechanism-Based Inactivators.8.3.1 Distinguishing Features of Mechanism-Based Inactivation.8.3.2 Determination of the Partition Ratio.8.3.3 Potential Clinical Advantages of Mechanism-Based Inactivators.8.3.4 Examples of Mechanism-Based Inactivators as Drugs.8.4 Use of Affinity Labels as Mechanistic Tools.8.5 Summary.References.Appendix 1. Kinetic of Biochemical Reactions.A1.1 The Law of Mass Action and Reaction Order.A1.2 First-Order Reaction Kinetics.A1.3 Second-Order Reaction Kinetics.A1.4 Pseudo-First-Order Reaction Conditions.A1.5 Approach to Equilibrium: An Example of the Kinetics of Reversible Reactions.References.Appendix 2. Derivation of the Enzyme-Ligand Binding Isotherm Equation.References.Appendix 3. Serial Dilution Schemes.Index.
Record Nr. UNINA-9910141602903321
Copeland Robert Allen  
Hoboken, N.J., : Wiley, c2013
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / by Robert A. Copeland
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / by Robert A. Copeland
Autore Copeland Robert Allen
Edizione [2nd ed.]
Pubbl/distr/stampa Hoboken, N.J., : Wiley, c2013
Descrizione fisica 1 online resource (572 p.)
Disciplina 615/.19
Soggetto topico Enzyme inhibitors - Therapeutic use - Testing
Drugs - Design
Enzyme inhibitors - Structure-activity relationships
ISBN 1-118-54039-5
1-299-24215-4
1-118-54040-9
1-118-54028-X
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Machine generated contents note: Foreword.Preface.Acknowledgments.1. Why Enzymes as Drug Targets?1.1 Enzymes Are Essentials for Life.1.2 Enzyme Structure and Catalysis.1.3 Permutations of Enzyme Structure During Catalysis.1.4 Other Reasons for Studying Enzymes.1.5 Summary.References.2. Enzyme Reaction Mechanisms.2.1 Initial Binding of Substrate.2.2 Noncovalent Forces in Reversible Ligand Binding to Enzymes.2.2.1 Electrostatic Forces.2.2.2 Hydrogen Bonds.2.2.3 Hydrophobic Forces.2.2.4 van der Waals Forces.2.3 Transformations of the Bond Substrate.2.3.1 Strategies for Transition State Stabilization.2.3.2 Enzyme Active Sites Are Most Complementary to the Transition State Structure.2.4 Steady State Analysis of Enzyme Kinetics.2.4.1 Factors Affecting the Steady State Kinetic Constants.2.5 Graphical Determination of kcat and KM2.6 Reactions Involving Multiple Substates.2.6.1 Bisubstrate Reaction Mechanisms.2.7 Summary.References.3. Reversible Modes of Inhibitor Interactions with Enzymes.3.1 Enzyme-Inhibitor Binding Equilibria.3.2 Competitive Inhibition.3.3 Noncompetitive Inhibition.3.3.1 Mutual Exclusively Studies.3.4 Uncompetitive Inhibition.3.5 Inhibition Modality in Bisubstrate Reactions.3.6 Value of Knowing Inhibitor Modality.3.6.1 Quantitative Comparisons of Inhibitor Affinity.3.6.2 Relating Ki to Binding Energy.3.6.3 Defining Target Selectivity by Ki Values.3.6.4 Potential Advantages and Disadvantages of Different Inhibition Modalities In Vivo.3.6.5 Knowing Inhibition Modality Is Important for Structure-Based Lead Organization.3.7 Summary.References.4. Assay Considerations for Compound Library Screening.4.1 Defining Inhibition Signal Robustness, and Hit Criteria.4.2 Measuring Initial Velocity.4.2.1 End-Point and Kinetic Readouts.4.2.2 Effects of Enzyme Concentration.4.3 Balanced Assay Conditions.4.3.1 Balancing Conditions for Multisubstrate Reactions.4.4 Order of Reagent Addition.4.5 Use of Natural Substrates and Enzymes.4.6 Coupled Enzyme Assays.4.7 Hit Validation and Progression.4.8 Summary.References.5. Lead Optimization and Structure-Activity Relationships for Reversible Inhibitors.5.1 Concentration-Response Plots and IC50 Determination.5.1.1 The Hill Coefficient.5.1.2 Graphing and Reporting Concentration-Response Data.5.2 Testing for Reversibility.5.3 Determining Reversible Inhibition Modality and Dissociation Constant.5.4 Comparing Relative Affinity.5.4.1 Compound Selectivity.5.5 Associating Cellular Effects with Target Enzyme Inhibition.5.5.1 Cellular Phenotype Should Be Consistent with Genetic Knockout or Knockdown of the Target Enzyme.5.5.2 Cellular Activity Should Require a Certain Affinity for the target Enzyme.5.5.3 Buildup of Substrate and/or Diminution of Product for the Target Enzyme Should Be Observed in Cells.5.5.4 Cellular Phenotype Should Be Reversed by Cell-Permeable Product or Downstream Metabolites of the Target Enzyme Activity.5.5.5 Mutation of the Target Enzyme Should Lead to Resistance or Hypersensitivity to Inhibitors.5.6 Summary.References.6. Slow Binding Inhibitors.6.1 Determining kobs: The Rate Constant for Onset of Inhibition.6.2 Mechanisms of Slow Binding Inhibition.6.3 Determination of Mechanism and Assessment of True Affinity.6.3.1 Potential Clinical Advantages of Slow Off-rate Inhibitors.6.4 Determining Inhibition Modality for Slow Binding Inhibitors.6.5 SAR for Slow Binding Inhibitors.6.6 Some Examples of Pharmacologically Interesting Slow Binding Inhibitors.6.6.1 Examples of Scheme B: Inhibitors of Zinc Peptidases and Proteases.6.6.2 Example of Scheme C: Inhibition of Dihydrofolate Reductase by Methotresate.6.6.3 Example of Scheme C: Inhibition of Calcineurin by FKBP-Inhibitor Complexes.6.6.4 Example of Scheme C When Ki* << Ki: Aspartyl Protease Inhibitors.6.6.5 Example of Scheme C When k6 Is Very Small: Selective COX2 Inhibitors.6.7 Summary.References.7. Tight Binding Inhibitors.7.1 Effects of Tight Binding Inhibition Concentration-Response Data.7.2 The IC50 Value Depends on Kiapp and [E]T.7.3 Morrison's Quadratic Equation for Fiting Concentration-Response Data for Tight Binding Inhibitors.7.3.1 Optimizing Conditions for Kiapp Determination Using Morrison's Equation.7.3.2 Limits on Kiapp Determinations.7.3.3 Use of a Cubic Equation When Both Substrate and Inhibitor Are Tight Binding.7.4 Determining Modality for Tight Binding Enzyme Inhibitors.7.5 Tight Binding Inhibitors Often Display Slow Binding Behavior.7.6 Practical Approaches to Overcoming the Tight Binding Limit in Determine Ki.7.7 Enzyme-Reaction Intermediate Analogues as Example of Tight Binding Inhibitors.7.7.1 Bisubstrate Analogues.7.7.2 Testing for Transition State Mimicry.7.8 Potential Clinical Advantages of Tight Binding Inhibitors.7.9 Determination of [E]T Using Tight Binding Inhibitors.7.10 Summary.References.8. Irreversible Enzyme Inactivators.8.1 Kinetic Evaluation of Irreversible Enzyme Inactivators.8.2 Affinity Labels.8.2.1 Quiescent Affinity Labels.8.2.2 Potential Liabilities of Affinity Labels as Drugs.8.3 Mechanism-Based Inactivators.8.3.1 Distinguishing Features of Mechanism-Based Inactivation.8.3.2 Determination of the Partition Ratio.8.3.3 Potential Clinical Advantages of Mechanism-Based Inactivators.8.3.4 Examples of Mechanism-Based Inactivators as Drugs.8.4 Use of Affinity Labels as Mechanistic Tools.8.5 Summary.References.Appendix 1. Kinetic of Biochemical Reactions.A1.1 The Law of Mass Action and Reaction Order.A1.2 First-Order Reaction Kinetics.A1.3 Second-Order Reaction Kinetics.A1.4 Pseudo-First-Order Reaction Conditions.A1.5 Approach to Equilibrium: An Example of the Kinetics of Reversible Reactions.References.Appendix 2. Derivation of the Enzyme-Ligand Binding Isotherm Equation.References.Appendix 3. Serial Dilution Schemes.Index.
Record Nr. UNINA-9910808406303321
Copeland Robert Allen  
Hoboken, N.J., : Wiley, c2013
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / Robert A. Copeland
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / Robert A. Copeland
Autore Copeland Robert Allen
Pubbl/distr/stampa Hoboken, N.J., : Wiley-Interscience, 2005
Descrizione fisica xvii, 271 p. : ill
Disciplina 615/.19
Collana Methods of biochemical analysis
Soggetto topico Enzyme inhibitors - Therapeutic use - Testing
Drugs - Design
Enzyme inhibitors - Structure-activity relationships
Soggetto genere / forma Electronic books.
ISBN 0-471-72327-4
1-280-25506-4
9786610255061
0-471-72326-6
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Record Nr. UNINA-9910449948503321
Copeland Robert Allen  
Hoboken, N.J., : Wiley-Interscience, 2005
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / Robert A. Copeland
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / Robert A. Copeland
Autore Copeland Robert Allen
Pubbl/distr/stampa Hoboken, N.J., : Wiley-Interscience, 2005
Descrizione fisica xvii, 271 p. : ill
Disciplina 615/.19
Collana Methods of biochemical analysis
Soggetto topico Enzyme inhibitors - Therapeutic use - Testing
Drugs - Design
Enzyme inhibitors - Structure-activity relationships
ISBN 0-471-72327-4
1-280-25506-4
9786610255061
0-471-72326-6
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Record Nr. UNINA-9910783520003321
Copeland Robert Allen  
Hoboken, N.J., : Wiley-Interscience, 2005
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / Robert A. Copeland
Evaluation of enzyme inhibitors in drug discovery [[electronic resource] ] : a guide for medicinal chemists and pharmacologists / / Robert A. Copeland
Autore Copeland Robert Allen
Edizione [1st ed.]
Pubbl/distr/stampa Hoboken, N.J., : Wiley-Interscience, 2005
Descrizione fisica xvii, 271 p. : ill
Disciplina 615/.19
Collana Methods of biochemical analysis
Soggetto topico Enzyme inhibitors - Therapeutic use - Testing
Drugs - Design
Enzyme inhibitors - Structure-activity relationships
ISBN 0-471-72327-4
1-280-25506-4
9786610255061
0-471-72326-6
Formato Materiale a stampa
Livello bibliografico Monografia
Lingua di pubblicazione eng
Nota di contenuto Intro -- Evaluation of Enzyme Inhibitors in Drug Discovery -- Contents -- Foreword -- Preface -- Acknowledgments -- 1. Why Enzymes as Drug Targets? -- 1.1 Enzymes Are Essential for Life -- 1.2 Enzyme Structure and Catalysis -- 1.3 Permutations of Enzyme Structure during Catalysis -- 1.4 Other Reasons for Studying Enzymes -- 1.5 Summary -- References -- 2. Enzyme Reaction Mechanisms -- 2.1 Initial Binding of Substrate -- 2.2 Noncovalent Forces in Reversible Ligand Binding to Enzymes -- 2.2.1 Electrostatic Forces -- 2.2.2 Hydrogen Bonds -- 2.2.3 Hydrophobic Forces -- 2.2.4 van der Waals Forces -- 2.3 Transformations of the Bound Substrate -- 2.3.1 Strategies for Transition State Stabilization -- 2.3.2 Enzyme Active Sites Are Most Complementary to the Transition State Structure -- 2.4 Steady State Analysis of Enzyme Kinetics -- 2.4.1 Factors Affecting the Steady State Kinetic Constants -- 2.5 Graphical Determination of k(cat) and K(M) -- 2.6 Reactions Involving Multiple Substrates -- 2.6.1 Bisubstrate Reaction Mechanisms -- 2.7 Summary -- References -- 3. Reversible Modes of Inhibitor Interactions with Enzymes -- 3.1 Enzyme-Inhibitor Binding Equilibria -- 3.2 Competitive Inhibition -- 3.3 Noncompetititive Inhibition -- 3.3.1 Mutual Exclusivity Studies -- 3.4 Uncompetitive Inhibition -- 3.5 Inhibition Modality in Bisubstrate Reactions -- 3.6 Value of Knowing Inhibitor Modality -- 3.6.1 Quantitative Comparisons of Inhibitor Affinity -- 3.6.2 Relating K(i) to Binding Energy -- 3.6.3 Defining Target Selectivity by K(i) Values -- 3.6.4 Potential Advantages and Disadvantages of Different Inhibition Modalities In Vivo -- 3.6.5 Knowing Inhibition Modality Is Important for Structure-Based Lead Optimization -- 3.7 Summary -- References -- 4. Assay Considerations for Compound Library Screening -- 4.1 Defining Inhibition, Signal Robustness, and Hit Criteria.
4.2 Measuring Initial Velocity -- 4.2.1 End-Point and Kinetic Readouts -- 4.2.2 Effects of Enzyme Concentration -- 4.2.3 Other Factors Affecting Initial Velocity -- 4.3 Balanced Assay Conditions -- 4.3.1 Balancing Conditions for Multisubstrate Reactions -- 4.4 Order of Reagent Addition -- 4.5 Use of Natural Substrates and Enzymes -- 4.6 Coupled Enzyme Assays -- 4.7 Hit Validation and Progression -- 4.8 Summary -- References -- 5. Lead Optimization and Structure-Activity Relationships for Reversible Inhibitors -- 5.1 Concentration-Response Plots and IC(50) Determination -- 5.1.1 The Hill Coefficient -- 5.1.2 Graphing and Reporting Concentration-Response Data -- 5.2 Testing for Reversibility -- 5.3 Determining Reversible Inhibition Modality and Dissociation Constant -- 5.4 Comparing Relative Affinity -- 5.4.1 Compound Selectivity -- 5.5 Associating Cellular Effects with Target Enzyme Inhibition -- 5.5.1 Cellular Phenotype Should Be Consistent with Genetic Knockout or Knockdown of the Target Enzyme -- 5.5.2 Cellular Activity Should Require a Certain Affinity for the Target Enzyme -- 5.5.3 Buildup of Substrate and/or Diminution of Product for the Target Enzyme Should Be Observed in Cells -- 5.5.4 Cellular Phenotype Should Be Reversed by Cell-Permeable Product or Downstream Metabolites of the Target Enzyme Activity -- 5.5.5 Mutation of the Target Enzyme Should Lead to Resistance or Hypersensitivity to Inhibitors -- 5.6 Summary -- References -- 6. Slow Binding Inhibitors -- 6.1 Determining k(obs): The Rate Constant for Onset of Inhibition -- 6.2 Mechanisms of Slow Binding Inhibition -- 6.3 Determination of Mechanism and Assessment of True Affinity -- 6.3.1 Potential Clinical Advantages of Slow Off-rate Inhibitors -- 6.4 Determining Inhibition Modality for Slow Binding Inhibitors -- 6.5 SAR for Slow Binding Inhibitors.
6.6 Some Examples of Pharmacologically Interesting Slow Binding Inhibitors -- 6.6.1 Examples of Scheme B: Inhibitors of Zinc Peptidases and Proteases -- 6.6.2 Example of Scheme C: Inhibition of Dihydrofolate Reductase by Methotrexate -- 6.6.3 Example of Scheme C: Inhibition of Calcineurin by FKBP-Inhibitor Complexes -- 6.6.4 Example of Scheme C When K*(i) < -- < -- K(i): Aspartyl Protease Inhibitors -- 6.6.5 Example of Scheme C When k(6) Is Very Small: Selective COX2 Inhibitors -- 6.7 Summary -- References -- 7. Tight Binding Inhibitors -- 7.1 Effects of Tight Binding Inhibition Concentration-Response Data -- 7.2 The IC(50) Value Depends on K(app)(i) and [E](T) -- 7.3 Morrison's Quadratic Equation for Fitting Concentration-Response Data for Tight Binding Inhibitors -- 7.3.1 Optimizing Conditions for K(app)(i) Determination Using Morrison's Equation -- 7.3.2 Limits on K(app)(i) Determinations -- 7.3.3 Use of a Cubic Equation When Both Substrate and Inhibitor Are Tight Binding -- 7.4 Determining Modality for Tight Binding Enzyme Inhibitors -- 7.5 Tight Binding Inhibitors Often Display Slow Binding Behavior -- 7.6 Practical Approaches to Overcoming the Tight Binding Limit in Determining K(i) -- 7.7 Enzyme-Reaction Intermediate Analogues as Examples of Tight Binding Inhibitors -- 7.7.1 Bisubstrate Analogues -- 7.7.2 Testing for Transition State Mimicry -- 7.8 Potential Clinical Advantages of Tight Binding Inhibitors -- 7.9 Determination of [E](T) Using Tight Binding Inhibitors -- 7.10 Summary -- References -- 8. Irreversible Enzyme Inactivators -- 8.1 Kinetic Evaluation of Irreversible Enzyme Inactivators -- 8.2 Affinity Labels -- 8.2.1 Quiescent Affinity Labels -- 8.2.2 Potential Liabilities of Affinity Labels as Drugs -- 8.3 Mechanism-Based Inactivators -- 8.3.1 Distinguishing Features of Mechanism-Based Inactivation.
8.3.2 Determination of the Partition Ratio -- 8.3.3 Potential Clinical Advantages of Mechanism-Based Inactivators -- 8.3.4 Examples of Mechanism-Based Inactivators as Drugs -- 8.4 Use of Affinity Labels as Mechanistic Tools -- 8.5 Summary -- References -- Appendix 1. Kinetics of Biochemical Reactions -- A1.1 The Law of Mass Action and Reaction Order -- A1.2 First-Order Reaction Kinetics -- A1.3 Second-Order Reaction Kinetics -- A1.4 Pseudo-First-Order Reaction Conditions -- A1.5 Approach to Equilibrium: An Example of the Kinetics of Reversible Reactions -- References -- Appendix 2. Derivation of the Enzyme-Ligand Binding Isotherm Equation -- References -- Appendix 3. Serial Dilution Schemes -- Index.
Record Nr. UNINA-9910827528903321
Copeland Robert Allen  
Hoboken, N.J., : Wiley-Interscience, 2005
Materiale a stampa
Lo trovi qui: Univ. Federico II
Opac: Controlla la disponibilità qui