{"product_id":"ligand-binding-basics-evaluating-intermolecular-affinity-specificity-stoichiometry-and-cooperativity-hardback-9781119878421","title":"Ligand-Binding Basics; Evaluating Intermolecular Affinity, Specificity, Stoichiometry, and Cooperativity (Hardback) 9781119878421","description":"\u003cfont face=\"Georgia\"\u003e\r\n\u003cp\u003e\u003cfont size=\"6\"\u003eLigand-Binding Basics\u003c\/font\u003e\u003cbr\u003e\r\n\u003cfont size=\"5\"\u003eEvaluating Intermolecular Affinity, Specificity, Stoichiometry, and Cooperativity\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\u003cp\u003e\u003cfont size=\"4\"\u003eJannette Carey (Author), Ethan Sample (Drawings by)\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e9781119878421, Wiley\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eHardback, published 16 October 2025\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e256 pages\u003cbr\u003e24.6 x 17.3 x 2 cm, 0.612 kg\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\r\n\r\n\r\n\u003cp align=\"justify\"\u003e\u003cstrong\u003e\u003cfont size=\"3\"\u003e\u003cp\u003e\u003cb\u003eA concise and accessible textbook covering ligand-binding theory in chemistry, biology, and drug development\u003c\/b\u003e \u003c\/p\u003e\n\u003cp\u003eIn \u003ci\u003eLigand-binding Basics: Evaluating Intermolecular Affinity, Specificity, Stoichiometry, and Cooperativity\u003c\/i\u003e, accomplished chemist Professor Jannette Carey introduces ligand binding in a thorough and practical way for those new to the topic, as well as anyone seeking a connection between theory and experiment. Using a minimum of mathematical formalism, this book offers analytical rigor while remaining accessible to non-specialist practitioners. It provides readers with the skills they need to analyze their own binding data or published results, helping them develop an intuitive grasp of ligand-binding phenomena integrated with structural and thermodynamic understanding. \u003c\/p\u003e\n\u003cp\u003eTopics covered include: \u003c\/p\u003e\n\u003cul\u003e\n\u003cli\u003eApplication of the principles of equilibrium, mass action, and mass balance to derive the basic equations that describe all binding processes\u003c\/li\u003e\n\u003cli\u003eRecommended approaches for plotting and graphical analysis of binding data\u003c\/li\u003e\n\u003cli\u003eStrategies for designing, analyzing, interpreting, and troubleshooting experiments from the perspective of ligand-binding theory\u003c\/li\u003e\n\u003cli\u003eReview of selected examples that illustrate integration of structural and thermodynamic analysis\u003c\/li\u003e\n\u003c\/ul\u003e \u003cp\u003ePerfect for students and educators in chemistry, biochemistry, molecular biology, and pharmaceutical science, \u003ci\u003eLigand-binding Basics\u003c\/i\u003e will also appeal to practitioners who aim to study ligand binding in any molecular system.\u003c\/p\u003e\u003c\/font\u003e\u003c\/strong\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003e\u003cp\u003eAbout the Cover xi\u003cbr\u003eIntroduction xiii\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 The Biology of Molecules 1\u003cbr\u003e\u003c\/b\u003eWhy Study Intermolecular Interactions Quantitatively? 1\u003cbr\u003eEquilibrium and Kinetics 2\u003cbr\u003eThermodynamic Definitions of Affinity and Specificity 3\u003cbr\u003eThe Affinity\/Specificity Map 6\u003cbr\u003eBiology Requires Optimization of Affinity and Specificity 8\u003cbr\u003eThe Special Case of Protein-DNA Interactions 8\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 General Theory for Reversible Ligand Binding 10\u003cbr\u003e\u003c\/b\u003eDefinition of Ligand and Titration 10\u003cbr\u003eAffinity, Specificity, Stoichiometry, and Cooperativity 10\u003cbr\u003eLigand-binding Theory: Relationship to Experiment 13\u003cbr\u003eGeneral Theory for Reversible Ligand Binding: Rooted in Chemical Equilibrium 14\u003cbr\u003eGeneral Theory for Reversible Ligand Binding: Quantitative Treatment 14\u003cbr\u003eThe Case of 1:1 Binding 15\u003cbr\u003eGeneral Theory for Reversible Ligand Binding: Conservation of Mass 17\u003cbr\u003eDefinition of ν 18\u003cbr\u003eThe Basic Equation for 1:1 Binding 19\u003cbr\u003eThe Single Most Important Thing You Can Learn in This Book 20\u003cbr\u003eThe Example of Heme Binding to Apocytochrome c 21\u003cbr\u003eThe Rectangular Hyperbola 22\u003cbr\u003eThe Binding Isotherm 23\u003cbr\u003ePlot of ν vs. [H f ] 24\u003cbr\u003eGeneral Theory for Reversible Ligand Binding: Role of Mass Action 25\u003cbr\u003ePlot of [AH]vs.[H t ] with Fixed K 27\u003cbr\u003eDetermination of K d from Experiment 28\u003cbr\u003ePlot of [AH]vs.[H t ] with Fixed [A t ] 29\u003cbr\u003eDetermining Molar Ratio from Experiment 29\u003cbr\u003eAbout Activity 31\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Graphical Analysis 33\u003cbr\u003e\u003c\/b\u003eLimitations of Direct Plots 33\u003cbr\u003eThe Semi-log Plot 34\u003cbr\u003eBreadth of the Semi-log Plot 36\u003cbr\u003eMyoglobin and Hemoglobin 38\u003cbr\u003eAdvantages of the Direct and Semi-log Plots of Binding Data 40\u003cbr\u003eLinear Transforms of the Basic Binding Equation 40\u003cbr\u003eCommon Linearizations 41\u003cbr\u003eRequirements of the Linear Regression Model 41\u003cbr\u003eA Linear Model May Misrepresent the Physical Process 43\u003cbr\u003eDeviations from Linearity Are Hard to Detect or Interpret 44\u003cbr\u003eLinear Transforms Distort Data Completeness 44\u003cbr\u003eLinear Transforms Invite – Even Require – Extrapolation 46\u003cbr\u003eLinear Transforms Falsely Promise Both K and Molar Ratio from a Single Dataset 47\u003cbr\u003eSummary about Linear Treatments of Binding Data 47\u003cbr\u003eSimulation Is Just as Good as Fitting, Given Realistic Experimental Errors 50\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Binding of Multiple Ligands 52\u003cbr\u003e\u003c\/b\u003eConservation of Mass Outside the 1:1 Case 52\u003cbr\u003eRedefine ν to Accommodate Any Molar Ratio 53\u003cbr\u003eAccounting for the Definition of Molecule 54\u003cbr\u003eGeneralizing to Integer Multiples of 1:1 54\u003cbr\u003eThe Langmuir Equation for Any Molar Ratio with Sites of Identical Affinity and No Cooperativity 56\u003cbr\u003eAdair Equation for Any Number of Binding Events 57\u003cbr\u003eThe Langmuir Equation vs. the Adair Equation 60\u003cbr\u003eThermodynamic Linkage 61\u003cbr\u003eTwo Classes of Sites with Different Affinities 62\u003cbr\u003eBinding Isotherms for Multiple Sites with Different Affinities 62\u003cbr\u003eSummary 66\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 How to Determine K d and Molar Ratio Experimentally 67\u003cbr\u003e\u003c\/b\u003eStoichiometric Titration First 68\u003cbr\u003eAmounts of Materials 69\u003cbr\u003eAssigning Partners 69\u003cbr\u003eChoice of Experimental Observables 70\u003cbr\u003eChoosing Solution Conditions 70\u003cbr\u003eHow Many Data Points? 71\u003cbr\u003eRange-Finding Stoichiometric Titration 72\u003cbr\u003eVisualizing Results 73\u003cbr\u003eRange-Finding Asymptotic Titration to Estimate K d 74\u003cbr\u003eData Analysis 75\u003cbr\u003ePracticalities about Experimental Error 75\u003cbr\u003eStatistical Approaches to Estimate the Breakpoint 76\u003cbr\u003eRefined Asymptotic Titration 76\u003cbr\u003eDesigning an Experiment to Refine K d 77\u003cbr\u003eCalculating Free Ligand Concentration 78\u003cbr\u003eRefining the Value of Molar Ratio 79\u003cbr\u003eExample of ArgR\/DNA Binding 79\u003cbr\u003ePlotting the Data 81\u003cbr\u003eDeriving K d from the Data 81\u003cbr\u003eSummary 81\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Cooperativity 83\u003cbr\u003e\u003c\/b\u003eFacilitated and Antagonized Binding 83\u003cbr\u003eFree Energy Definition of Cooperative Binding 84\u003cbr\u003eChemical Potential Diagram for Cooperative Binding 86\u003cbr\u003eCooperativity as Non-additivity 87\u003cbr\u003eReciprocity of Cooperative Effects 88\u003cbr\u003eLimitations of Linear Transforms for Cooperative Interactions 88\u003cbr\u003eMicroscopic View of Species Distribution 89\u003cbr\u003eHomotropic and Heterotropic Cooperativity 90\u003cbr\u003eCooperativity Affects Specificity as Well as Affinity 92\u003cbr\u003eCooperativity Is the Third Axis of the Affinity\/Specificity Map 94\u003cbr\u003eQuantifying Homotropic Cooperativity 95\u003cbr\u003eNegative Homotropic Cooperativity 95\u003cbr\u003eA Practical Advantage of Negative Cooperativity 97\u003cbr\u003ePositive Cooperativity and the Ligand Concentration Interval 97\u003cbr\u003eImportance of Individual-site Isotherms and Species Distribution 100\u003cbr\u003eSpecies Distributions by Specialized Experimental Methods 101\u003cbr\u003eThe Many Forms of Cooperativity 103\u003cbr\u003eEmergent Properties 103\u003cbr\u003eConnectivity and Search Entropy 104\u003cbr\u003eBreakdown of Additivity in Complex Systems 105\u003cbr\u003eStatistical Effects 107\u003cbr\u003eRelevance of Non-additivity for Analysis of Mutations 110\u003cbr\u003eUniversality and Promiscuity of Cooperativity 111\u003cbr\u003eProteins as Gestalt Objects 113\u003cbr\u003eSummary 115\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Theoretical and Method-specific Troubleshooting 116\u003cbr\u003e\u003c\/b\u003eEquilibrium and Nonequilibrium Methods 116\u003cbr\u003eAccessible Concentration Ranges Limit Accessible K d Values 116\u003cbr\u003eSignal from Ligand or Target? 118\u003cbr\u003eSeparation-based Methods 118\u003cbr\u003eFilter Binding 119\u003cbr\u003eGel Retardation or EMSA 120\u003cbr\u003eGel Filtration 121\u003cbr\u003eHummel and Dreyer Chromatography 121\u003cbr\u003eEquilibrium Dialysis 122\u003cbr\u003eUV Absorbance 123\u003cbr\u003eCD Spectroscopy 123\u003cbr\u003eFluorescence 124\u003cbr\u003eNMR 124\u003cbr\u003eITC 125\u003cbr\u003eAUC 129\u003cbr\u003eSPR 129\u003cbr\u003eMS 131\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Allostery 133\u003cbr\u003e\u003c\/b\u003eAn Historical Overview 133\u003cbr\u003eFacilitated Binding 135\u003cbr\u003eElaboration of the MWC Model 136\u003cbr\u003eRelaxed Monomers and Tense Multimers 136\u003cbr\u003ePositive Homotropic Cooperativity Only 137\u003cbr\u003eArtifactual Origins of Affinity Heterogeneity 138\u003cbr\u003eRelaxation of Multimers by Ligand Binding 138\u003cbr\u003eKoshland’s Sequential (Asymmetric) Model 140\u003cbr\u003eG3Pase Was Heterogeneous, Not Negatively Cooperative 141\u003cbr\u003eMany Models Fit the Hemoglobin Data 142\u003cbr\u003eAdvantages of Negative Cooperativity for Molecular Insight 143\u003cbr\u003eBiology of Negative Cooperativity 145\u003cbr\u003eStructural Analysis Cannot Solve Allostery 146\u003cbr\u003eAllostery without Cooperativity 147\u003cbr\u003eSummary 148\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Lessons on Affinity and Specificity from Host\/Guest Chemistry 149\u003cbr\u003e\u003c\/b\u003e2D Representations of 3D Objects 149\u003cbr\u003eEarly Hosts Were Linear and Flexible 150\u003cbr\u003eDesign of Molecular Properties 151\u003cbr\u003eVery Weak Affinity and No Detectable Specificity 151\u003cbr\u003eLater Hosts Pre-organized in Bound Conformation 152\u003cbr\u003eEnormous Gains in Affinity and Specificity 152\u003cbr\u003eBonds between Host and Guest Are Identical 153\u003cbr\u003eLessons from the Host\/Guest Chemistry 153\u003cbr\u003eRational Design of Affinity and Specificity 153\u003cbr\u003eAffinity and Specificity Accrue in Parallel 155\u003cbr\u003eCryptic Contributions Can Dominate Binding 156\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Reconciling Structure and Thermodynamics in Molecular Interactions 157\u003cbr\u003e\u003c\/b\u003eThermodynamics of Molecular Interactions 158\u003cbr\u003eStructural Analysis of Bonding Does Not Predict Binding 160\u003cbr\u003eThe Goldilocks Region of Affinity\/Specificity Space 162\u003cbr\u003eConformational Rearrangement upon Binding Decouples Affinity and Specificity 163\u003cbr\u003eA Reservoir of Adaptability 164\u003cbr\u003eNo Simple Reconciliation of Structural and Energetic Views 165\u003cbr\u003eImplications for Drug Design 166\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Applications in Modern Drug Development 167\u003cbr\u003e\u003c\/b\u003eBackground 167\u003cbr\u003eTechnological Developments 167\u003cbr\u003eCrystal Structures 168\u003cbr\u003eTrapped High-energy States 168\u003cbr\u003eAnother Example 171\u003cbr\u003eComputational Methods 175\u003cbr\u003eHigh-throughput Assays 177\u003cbr\u003eDruggability 178\u003cbr\u003eIrrational Drug Design 180\u003cbr\u003eA New Workflow 181\u003c\/p\u003e \u003cp\u003eAppendix A Ligand-binding Study Questions 182\u003cbr\u003eAppendix B Thought Experiments 195\u003cbr\u003eAppendix C Derivations 197\u003cbr\u003eAppendix D Simulation and Fitting 201\u003cbr\u003eSimulation 201\u003cbr\u003eFitting 203\u003cbr\u003eAppendix E About the Hill Equation 208\u003cbr\u003eDeriving the Hill Equation 208\u003cbr\u003eThe Hill Equation as a Limit of the Adair Equation 209\u003cbr\u003eOn Applying the Hill Equation to Quantify Cooperativity 210\u003cbr\u003eAppendix F Stereo Viewing 212\u003cbr\u003eBibliography 215\u003cbr\u003eIndex 227\u003c\/p\u003e\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\u003cp\u003e\u003cfont size=\"3\"\u003eSubject Areas: Chemistry [\u003ca title=\"See our other books on Chemistry\" href=\"https:\/\/freshlyprintedbooks.co.uk\/search?q=%22Chemistry%20%5BPN%5D%22\"\u003ePN\u003c\/a\u003e]\u003c\/font\u003e\u003c\/p\u003e\r\n\r\n\r\n\u003c\/font\u003e","brand":"Wiley","offers":[{"title":"Brand New","offer_id":52501136867608,"sku":"9781119878421","price":73.75,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0730\/2037\/5320\/files\/9781119878421.jpg?v=1786211881","url":"https:\/\/freshlyprintedbooks.co.uk\/products\/ligand-binding-basics-evaluating-intermolecular-affinity-specificity-stoichiometry-and-cooperativity-hardback-9781119878421","provider":"Freshly Printed Books","version":"1.0","type":"link"}