Biochemistry: A Short Course

About this Book
	Cover Page
	Title Page
	Copyright Page
	Dedication
	About the Authors
	Preface
	Acknowledgments
	Brief Contents
	Contents
Section 1 Biochemistry Helps Us to Understand Our World
	Chapter 1 Biochemistry and the Unity of Life
		1.1 Living Systems Require a Limited Variety of Atoms and Molecules
		1.2 There Are Four Major Classes of Biomolecules
			Proteins Are Highly Versatile Biomolecules
			Nucleic Acids Are the Information Molecules of the Cell
			Lipids Are a Storage Form of Fuel and Serve as a Barrier
			Carbohydrates Are Fuels and Informational Molecules
		1.3 The Central Dogma Describes the Basic Principles of Biological Information Transfer
		1.4 Membranes Define the Cell and Carry Out Cellular Functions
			Biochemical Functions Are Sequestered in Cellular Compartments
			Some Organelles Process and Sort Proteins and Exchange Material with the Environment
		Summary
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 2 Water, Weak Bonds, and the Generation of Order Out of Chaos
		2.1 Thermal Motions Power Biological Interactions
		2.2 Biochemical Interactions Take Place in an Aqueous Solution
		2.3 Weak Interactions Are Important Biochemical Properties
			Electrostatic Interactions Are Between Electrical Charges
			Hydrogen Bonds Form Between an Electronegative Atom and Hydrogen
			van der Waals Interactions Depend on Transient Asymmetry in Electrical Charge
			Weak Bonds Permit Repeated Interactions
		2.4 Hydrophobic Molecules Cluster Together
			Membrane Formation Is Powered by the Hydrophobic Effect
			Protein Folding Is Powered by the Hydrophobic Effect
			Functional Groups Have Specific Chemical Properties
		2.5 pH Is an Important Parameter of Biochemical Systems
			Water Ionizes to a Small Extent
			An Acid Is a Proton Donor, Whereas a Base Is a Proton Acceptor
			Acids Have Differing Tendencies to Ionize
			Buffers Resist Changes in pH
			Buffers Are Crucial in Biological Systems
			Making Buffers Is a Common Laboratory Practice
		Summary
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 2 Protein composition and structure
	Chapter 3 Amino Acids Two Different Ways of Depicting Biomolecules Will Be Used
		Two Different Ways of Depicting Biomolecules Will Be Used
		3.1 Proteins Are Built from a Repertoire of 20 Amino Acids
			Most Amino Acids Exist in Two Mirror-Image Forms
			All Amino Acids Have at Least Two Charged Groups
		3.2 Amino Acids Contain a Wide Array of Functional Groups
			Hydrophobic Amino Acids Have Mainly Hydrocarbon Side Chains
			Polar Amino Acids Have Side Chains That Contain an Electronegative Atom
			Positively Charged Amino Acids Are Hydrophilic
			Negatively Charged Amino Acids Have Acidic Side Chains
			The Ionizable Side Chains Enhance Reactivity and Bonding
		3.3 Essential Amino Acids Must Be Obtained from the Diet
		Summary
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
	Chapter 4 Protein Three-Dimensional Structure
		4.1 Primary Structure: Amino Acids Are Linked by Peptide Bonds to Form Polypeptide Chains
			Proteins Have Unique Amino Acid Sequences Specified by Genes
			Polypeptide Chains Are Flexible Yet Conformationally Restricted
		4.2 Secondary Structure: Polypeptide Chains Can Fold into Regular Structures
			The Alpha Helix Is a Coiled Structure Stabilized by Intrachain Hydrogen Bonds
			Beta Sheets Are Stabilized by Hydrogen Bonding Between Polypeptide Strands
			Polypeptide Chains Can Change Direction by Making Reverse Turns and Loops
			Fibrous Proteins Provide Structural Support for Cells and Tissues
		4.3 Tertiary Structure: Water-Soluble Proteins Fold into Compact Structures
			Myoglobin Illustrates the Principles of Tertiary Structure
			The Tertiary Structure of Many Proteins Can Be Divided into Structural and Functional Units
		4.4 Quaternary Structure: Multiple Polypeptide Chains Can Assemble into a Single Protein
		4.5 The Amino Acid Sequence of a Protein Determines Its Three-Dimensional Structure
			Proteins Fold by the Progressive Stabilization of Intermediates Rather Than by Random Search
			Some Proteins Are Intrinsically Disordered and Can Exist in Multiple Conformations
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
	Chapter 5 Techniques in Protein Biochemistry
		5.1 The Proteome Is the Functional Representation of the Genome
		5.2 The Purification of a Protein Is the First Step in Understanding Its Function
			Proteins Can Be Purified on the Basis of Differences in Their Chemical Properties
			Proteins Must Be Removed from the Cell to Be Purified
			Proteins Can Be Purified According to Solubility, Size, Charge, and Binding Affinity
			Proteins Can Be Separated by Gel Electrophoresis and Displayed
			A Purification Scheme Can Be Quantitatively Evaluated
		5.3 Immunological Techniques Are Used to Purify and Characterize Proteins
			Centrifugation Is a Means of Separating Proteins
			Gradient Centrifugation Provides an Assay for the Estradiol–Receptor Complex
			Antibodies to Specific Proteins Can Be Generated
			Monoclonal Antibodies with Virtually Any Desired Specificity Can Be Readily Prepared
			The Estrogen Receptor Can Be Purified by Immunoprecipitation
			Proteins Can Be Detected and Quantified with the Use of an Enzyme-Linked Immunosorbent Assay
			Western Blotting Permits the Detection of Proteins Separated by Gel Electrophoresis
		5.4 Determination of Primary Structure Facilitates an Understanding of Protein Function
			Mass Spectrometry Can Be Used to Determine a Protein’s Mass, Identity, and Sequence
				Protein Mass
				Protein Identity
				Protein Sequence
			Amino Acid Sequences Are Sources of Many Kinds of Insight
		Summary
		Apendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 3 Basic Concepts and Kinetics of Enzymes
	Chapter 6 Basic Concepts of Enzyme Action
		6.1 Enzymes Are Powerful and Highly Specific Catalysts
			Proteolytic Enzymes Illustrate the Range of Enzyme Specificity
			There Are Six Major Classes of Enzymes
		6.2 Many Enzymes Require Cofactors for Activity
		6.3 Gibbs Free Energy Is a Useful Thermodynamic Function for Understanding Enzymes
			The Free-Energy Change Provides Information About the Spontaneity but Not the Rate of a Reaction
			The Standard Free-Energy Change of a Reaction Is Related to the Equilibrium Constant
			Enzymes Alter the Reaction Rate but Not the Reaction Equilibrium
		6.4 Enzymes Facilitate the Formation of the Transition State
			The Formation of an Enzyme–Substrate Complex Is the First Step in Enzymatic Catalysis
			The Active Sites of Enzymes Have Some Common Features
			The Binding Energy Between Enzyme and Substrate Is Important for Catalysis
			Transition-State Analogs Are Potent Inhibitors of Enzymes
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
	Chapter 7 Kinetics and Regulation
		7.1 Kinetics Is the Study of Reaction Rates
		7.2 The Michaelis–Menten Model Describes the Kinetics of Many Enzymes
			KM and Vmax Values Can Be Determined by Several Means
			KM and Vmax Values Are Important Enzyme Characteristics
			kcat/KM Is a Measure of Catalytic Efficiency
			Most Biochemical Reactions Include Multiple Substrates
				Sequential reactions
				Double-displacement (ping-pong) reactions
		7.3 Allosteric Enzymes Are Catalysts and Information Sensors
			Allosteric Enzymes Are Regulated by Products of the Pathways Under Their Control
			Allosterically Regulated Enzymes Do Not Conform to Michaelis–Menten Kinetics
			Allosteric Enzymes Depend on Alterations in Quaternary Structure
			Regulator Molecules Modulate the T R Equilibrium
			The Sequential Model Also Can Account for Allosteric Effects
		7.4 Enzymes Can Be Studied One Molecule at a Time
		Summary
		Appendix: Derivation of the Michaelis–Menten Equation
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 8 Mechanisms and Inhibitors
		8.1 A Few Basic Catalytic Strategies Are Used by Many Enzymes
		8.2 Enzyme Activity Can Be Modulated by Temperature, pH, and Inhibitory Molecules
			Temperature Enhances the Rate of Enzyme-Catalyzed Reactions
			Most Enzymes Have an Optimal pH
			Enzymes Can Be Inhibited by Specific Molecules
			Reversible Inhibitors Are Kinetically Distinguishable
			Irreversible Inhibitors Can Be Used to Map the Active Site
		8.3 Chymotrypsin Illustrates Basic Principles of Catalysis and Inhibition
			Serine 195 Is Required for Chymotrypsin Activity
			Chymotrypsin Action Proceeds in Two Steps Linked by a Covalently Bound Intermediate
			The Catalytic Role of Histidine 57 Was Demonstrated by Affinity Labeling
			Serine Is Part of a Catalytic Triad That Includes Histidine and Aspartic Acid
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 9 Hemoglobin, an Allosteric Protein
		9.1 Hemoglobin Displays Cooperative Behavior
		9.2 Myoglobin and Hemoglobin Bind Oxygen in Heme Groups
		9.3 Hemoglobin Binds Oxygen Cooperatively
		9.4 An Allosteric Regulator Determines the Oxygen Affinity of Hemoglobin
		9.5 Hydrogen Ions and Carbon Dioxide Promote the Release of Oxygen
		9.6 Mutations in Genes Encoding Hemoglobin Subunits Can Result in Disease
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
Section 4 Carbohydrates and Lipids
	Chapter 10 Carbohydrates
		10.1 Monosaccharides Are the Simplest Carbohydrates
			Many Common Sugars Exist in Cyclic Forms
			Pyranose and Furanose Rings Can Assume Different Conformations
			Monosaccharides Are Joined to Alcohols and Amines Through Glycosidic Bonds
		10.2 Monosaccharides Are Linked to Form Complex Carbohydrates
			Specific Enzymes Are Responsible for Oligosaccharide Assembly
			Sucrose, Lactose, and Maltose Are the Common Disaccharides
			Glycogen and Starch Are Storage Forms of Glucose
			Cellulose, a Structural Component of Plants, Is Made of Chains of Glucose
		10.3 Carbohydrates Are Attached to Proteins to Form Glycoproteins
			Carbohydrates May Be Linked to Asparagine, Serine, or Threonine Residues of Proteins
			Proteoglycans, Composed of Polysaccharides and Protein, Have Important Structural Roles
		10.4 Lectins Are Specific Carbohydrate-Binding Proteins
			Lectins Promote Interactions Between Cells
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 11 Lipids
		11.1 Fatty Acids Are a Main Source of Fuel
			Fatty Acids Vary in Chain Length and Degree of Unsaturation
		11.2 Triacylglycerols Are the Storage Form of Fatty Acids
		11.3 There Are Three Common Types of Membrane Lipids
			Phospholipids Are the Major Class of Membrane Lipids
			Membrane Lipids Can Include Carbohydrates
			Steroids Are Lipids That Have a Variety of Roles
			Membrane Lipids Contain a Hydrophilic and a Hydrophobic Moiety
			Some Proteins Are Modified by the Covalent Attachment of Hydrophobic Groups
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 5 Cell Membranes, Channels, Pumps, and Receptors
	Chapter 12 Membrane Structure and Function
		12.1 Phospholipids and Glycolipids Form Bimolecular Sheets
			Lipid Bilayers Are Highly Impermeable to Ions and Most Polar Molecules
		12.2 Membrane Fluidity Is Controlled by Fatty Acid Composition and Cholesterol Content
		12.3 Proteins Carry Out Most Membrane Processes
			Proteins Associate with the Lipid Bilayer in a Variety of Ways
		12.4 Lipids and Many Membrane Proteins Diffuse Laterally in the Membrane
		12.5 A Major Role of Membrane Proteins Is to Function as Transporters
			The Na+-K+ ATPase Is an Important Pump in Many Cells
			Secondary Transporters Use One Concentration Gradient to Power the Formation of Another
			Specific Channels Can Rapidly Transport Ions Across Membranes
			The Structure of the Potassium Ion Channel Reveals the Basis of Ion Specificity
			The Structure of the Potassium Ion Channel Explains Its Rapid Rate of Transport
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 13 Signal-Transduction Pathways
		13.1 Signal Transduction Depends on Molecular Circuits
		13.2 Receptor Proteins Transmit Information into the Cell
			Seven-Transmembrane-Helix Receptors Change Conformation in Response to Ligand Binding and Activate G Proteins
			Ligand Binding to 7TM Receptors Leads to the Activation of G Proteins
			Activated G Proteins Transmit Signals by Binding to Other Proteins
			Cyclic AMP Stimulates the Phosphorylation of Many Target Proteins by Activating Protein Kinase A
			G Proteins Spontaneously Reset Themselves Through GTP Hydrolysis
			The Hydrolysis of Phosphatidylinositol Bisphosphate by Phospholipase C Generates Two Second Messengers
		13.3 Some Receptors Dimerize in Response to Ligand Binding and Recruit Tyrosine Kinases
			Receptor Dimerization May Result in Tyrosine Kinase Recruitment
			Ras Belongs to Another Class of Signaling G Proteins
		13.4 Metabolism in Context: Insulin Signaling Regulates Metabolism
			The Insulin Receptor Is a Dimer That Closes Around a Bound Insulin Molecule
			The Activated Insulin-Receptor Kinase Initiates a Kinase Cascade
			Insulin Signaling Is Terminated by the Action of Phosphatases
		13.5 Calcium Ion Is a Ubiquitous Cytoplasmic Messenger
		13.6 Defects in Signaling Pathways Can Lead to Diseases
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 6 Basic Concepts and Design of Metabolism
	Chapter 14 Digestion: Turning a Meal into Cellular Biochemicals
		14.1 Digestion Prepares Large Biomolecules for Use in Metabolism
			Most Digestive Enzymes Are Secreted as Inactive Precursors
		14.2 Proteases Digest Proteins into Amino Acids and Peptides
			Protein Digestion Continues in the Intestine
		14.3 Dietary Carbohydrates Are Digested by Alpha-Amylase
		14.4 The Digestion of Lipids Is Complicated by Their Hydrophobicity
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
	Chapter 15 Metabolism: Basic Concepts and Design
		15.1 Energy Is Required to Meet Three Fundamental Needs
		15.2 Metabolism Is Composed of Many Interconnecting Reactions
			Metabolism Consists of Energy-Yielding Reactions and Energy-Requiring Reactions
			A Thermodynamically Unfavorable Reaction Can Be Driven by a Favorable Reaction
		15.3 ATP Is the Universal Currency of Free Energy
			ATP Hydrolysis Is Exergonic
			ATP Hydrolysis Drives Metabolism by Shifting the Equilibrium of Coupled Reactions
			The High Phosphoryl-Transfer Potential of ATP Results from Structural Differences Between ATP and Its Hydrolysis Products
			Phosphoryl-Transfer Potential Is an Important Form of Cellular Energy Transformation
			Phosphates Play a Prominent Role in Biochemical Processes
			ATP May Have Roles Other Than in Energy and Signal Transduction
		15.4 The Oxidation of Carbon Fuels Is an Important Source of Cellular Energy
			Carbon Oxidation Is Paired with a Reduction
			Compounds with High Phosphoryl-Transfer Potential Can Couple Carbon Oxidation to ATP Synthesis
		15.5 Metabolic Pathways Contain Many Recurring Motifs
			Activated Carriers Exemplify the Modular Design and Economy of Metabolism
			Many Activated Carriers Are Derived from Vitamins
		15.6 Metabolic Processes Are Regulated in Three Principal Ways
			The Amounts of Enzymes Are Controlled
			Catalytic Activity Is Regulated
			The Accessibility of Substrates Is Regulated
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
Section 7 Glycolysis and Gluconeogenesis
	Chapter 16 Glycolysis
		16.1 Glycolysis Is an Energy-Conversion Pathway
			The Enzymes of Glycolysis Are Associated with One Another
			Glycolysis Can Be Divided into Two Parts
			Hexokinase Traps Glucose in the Cell and Begins Glycolysis
			Fructose 1,6-Bisphosphate Is Generated from Glucose 6-Phosphate
			The Oxidation of an Aldehyde Powers the Formation of a Compound Having High Phosphoryl-Transfer Potential
			ATP Is Formed by Phosphoryl Transfer from 1,3-Bisphosphoglycerate
			Additional ATP Is Generated with the Formation of Pyruvate
			Two ATP Molecules Are Formed in the Conversion of Glucose into Pyruvate
		16.2 NAD+ Is Regenerated from the Metabolism of Pyruvate
			Fermentations Are a Means of Oxidizing NADH
		16.3 Fructose and Galactose Are Converted into Glycolytic Intermediates
			Fructose Is Converted into Glycolytic Intermediates by Fructokinase
			Galactose Is Converted into Glucose 6-Phosphate
		16.4 The Glycolytic Pathway Is Tightly Controlled
			Glycolysis in Muscle Is Regulated by Feedback Inhibition to Meet the Need for ATP
			The Regulation of Glycolysis in the Liver Corresponds to the Biochemical Versatility of the Liver
			A Family of Transporters Enables Glucose to Enter and Leave Animal Cells
		16.5 Metabolism in Context: Glycolysis Helps Pancreatic Beta Cells Sense Glucose
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 17 Gluconeogenesis
		17.1 Glucose Can Be Synthesized from Noncarbohydrate Precursors
			Gluconeogenesis Is Not a Complete Reversal of Glycolysis
			The Conversion of Pyruvate into Phosphoenolpyruvate Begins with the Formation of Oxaloacetate
			Oxaloacetate Is Shuttled into the Cytoplasm and Converted into Phosphoenolpyruvate
			The Conversion of Fructose 1,6-Bisphosphate into Fructose 6-Phosphate and Orthophosphate Is an Irreversible Step
			The Generation of Free Glucose Is an Important Control Point
			Six High-Transfer-Potential Phosphoryl Groups Are Spent in Synthesizing Glucose from Pyruvate
		17.2 Gluconeogenesis and Glycolysis Are Reciprocally Regulated
			Energy Charge Determines Whether Glycolysis or Gluconeogenesis Will Be More Active
			The Balance Between Glycolysis and Gluconeogenesis in the Liver Is Sensitive to Blood-Glucose Concentration
		17.3 Metabolism in Context: Precursors Formed by Muscle Are Used by Other Organs
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 8 The Citric Acid Cycle
	Chapter 18 Preparation for the Cycle
		18.1 Pyruvate Dehydrogenase Forms Acetyl Coenzyme A from Pyruvate
			The Synthesis of Acetyl Coenzyme A from Pyruvate Requires Three Enzymes and Five Coenzymes
			Flexible Linkages Allow Lipoamide to Move Between Different Active Sites
		18.2 The Pyruvate Dehydrogenase Complex Is Regulated by Two Mechanisms
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 19 Harvesting Electrons from the Cycle
		19.1 The Citric Acid Cycle Consists of Two Stages
		19.2 Stage One Oxidizes Two Carbon Atoms to Gather Energy-Rich Electrons
			Citrate Synthase Forms Citrate from Oxaloacetate and Acetyl Coenzyme A
			The Mechanism of Citrate Synthase Prevents Undesirable Reactions
			Citrate Is Isomerized into Isocitrate
			Isocitrate Is Oxidized and Decarboxylated to Alpha-Ketoglutarate
			Succinyl Coenzyme A Is Formed by the Oxidative Decarboxylation of Alpha-Ketoglutarate
		19.3 Stage Two Regenerates Oxaloacetate and Harvests Energy-Rich Electrons
			A Compound with High Phosphoryl-Transfer Potential Is Generated from Succinyl Coenzyme A
			Succinyl Coenzyme A Synthetase Transforms Types of Biochemical Energy
			Oxaloacetate Is Regenerated by the Oxidation of Succinate
			The Citric Acid Cycle Produces High-Transfer-Potential Electrons, an ATP, and Carbon Dioxide
		19.4 The Citric Acid Cycle Is Regulated
			The Citric Acid Cycle Is Controlled at Several Points
			The Citric Acid Cycle Is a Source of Biosynthetic Precursors
			The Citric Acid Cycle Must Be Capable of Being Rapidly Replenished
		19.5 The Glyoxylate Cycle Enables Plants and Bacteria to Convert Fats into Carbohydrates
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 9 Oxidative Phosphorylation
	Chapter 20 The Electron-Transport Chain
		20.1 Oxidative Phosphorylation in Eukaryotes Takes Place in Mitochondria
			Mitochondria Are Bounded by a Double Membrane
		20.2 Oxidative Phosphorylation Depends on Electron Transfer
			The Electron-Transfer Potential of an Electron Is Measured as Redox Potential
			Electron Flow Through the Electron-Transport Chain Creates a Proton Gradient
			The Electron-Transport Chain Is a Series of Coupled Oxidation−Reduction Reactions
		20.3 The Respiratory Chain Consists of Proton Pumps and a Physical Link to the Citric Acid Cycle
			The High-Potential Electrons of NADH Enter the Respiratory Chain at NADH-Q Oxidoreductase
			Ubiquinol Is the Entry Point for Electrons from FADH2 of Flavoproteins
			Electrons Flow from Ubiquinol to Cytochrome c Through Q-Cytochrome c Oxidoreductase
			The Q Cycle Funnels Electrons from a Two-Electron Carrier to a One-Electron Carrier and Pumps Protons
			Cytochrome c Oxidase Catalyzes the Reduction of Molecular Oxygen to Water
			Most of the Electron Transport Chain Is Organized into a Complex Called the Respirasome
			Toxic Derivatives of Molecular Oxygen Such as Superoxide Radical Are Scavenged by Protective Enzymes
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 21 The Electron-Transport Chain
		21.1 A Proton Gradient Powers the Synthesis of ATP
			ATP Synthase Is Composed of a Proton-Conducting Unit and a Catalytic Unit
			Proton Flow Through ATP Synthase Leads to the Release of Tightly Bound ATP
			Rotational Catalysis Is the World’s Smallest Molecular Motor
			Proton Flow Around the c Ring Powers ATP Synthesis
		21.2 Shuttles Allow Movement Across Mitochondrial Membranes
			Electrons from Cytoplasmic NADH Enter Mitochondria by Shuttles
			The Entry of ADP into Mitochondria Is Coupled to the Exit of ATP
			Mitochondrial Transporters Allow Metabolite Exchange Between the Cytoplasm and Mitochondria
		21.3 Cellular Respiration Is Regulated by the Need for ATP
			The Complete Oxidation of Glucose Yields About 30 Molecules of ATP
			The Rate of Oxidative Phosphorylation Is Determined by the Need for ATP
			Power Transmission by Proton Gradients Is a Central Motif of Bioenergetics
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 10 The Light Reactions of Photosynthesis and the Calvin Cycle
	Chapter 22 The Light Reactions
		22.1 Photosynthesis Takes Place in Chloroplasts
		22.2 Photosynthesis Transforms Light Energy into Chemical Energy
			Chlorophyll Is the Primary Light Acceptor in Most Photosynthetic Systems
			Light-Harvesting Complexes Enhance the Efficiency of Photosynthesis
		22.3 Two Photosystems Generate a Proton Gradient and NADPH
			Photosystem I Uses Light Energy to Generate Reduced Ferredoxin, a Powerful Reductant
			Photosystem II Transfers Electrons to Photosystem I and Generates a Proton Gradient
			Cytochrome b6f Links Photosystem II to Photosystem I
			The Oxidation of Water Achieves Oxidation–Reduction Balance and Contributes Protons to the Proton Gradient
		22.4 A Proton Gradient Drives ATP Synthesis
			The ATP Synthase of Chloroplasts Closely Resembles That of Mitochondria
			The Activity of Chloroplast ATP Synthase Is Regulated
			Cyclic Electron Flow Through Photosystem I Leads to the Production of ATP Instead of NADPH
			The Absorption of Eight Photons Yields One O2, Two NADPH, and Three ATP Molecules
			The Components of Photosynthesis Are Highly Organized
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
	Chapter 23 The Calvin Cycle
		23.1 The Calvin Cycle Synthesizes Hexoses from Carbon Dioxide and Water
			Carbon Dioxide Reacts with Ribulose 1,5-Bisphosphate to Form Two Molecules of 3-Phosphoglycerate
			Hexose Phosphates Are Made from Phosphoglycerate, and Ribulose 1,5-bisphosphate Is Regenerated
			Three Molecules of ATP and Two Molecules of NADPH Are Used to Bring Carbon Dioxide to the Level of a Hexose
			Starch and Sucrose Are the Major Carbohydrate Stores in Plants
		23.2 The Calvin Cycle Is Regulated by the Environment
			Thioredoxin Plays a Key Role in Regulating the Calvin Cycle
			Rubisco Also Catalyzes a Wasteful Oxygenase Reaction
			The C4 Pathway of Tropical Plants Accelerates Photosynthesis by Concentrating Carbon Dioxide
			Crassulacean Acid Metabolism Permits Growth in Arid Ecosystems
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 11 Glycogen Metabolism and the Pentose Phosphate Pathway
	Chapter 24 Glycogen Degradation
		24.1 Glycogen Breakdown Requires Several Enzymes
			Phosphorylase Cleaves Glycogen to Release Glucose 1-phosphate
			A Debranching Enzyme Also Is Needed for the Breakdown of Glycogen
			Phosphoglucomutase Converts Glucose 1-Phosphate into Glucose 6-Phosphate
			Liver Contains Glucose 6-Phosphatase, a Hydrolytic Enzyme Absent from Muscle
		24.2 Phosphorylase Is Regulated by Allosteric Interactions and Reversible Phosphorylation
			Liver Phosphorylase Produces Glucose for Use by Other Tissues
			Muscle Phosphorylase Is Regulated by the Intracellular Energy Charge
			Biochemical Characteristics of Muscle Fiber Types Differ
			Phosphorylation Promotes the Conversion of Phosphorylase b to Phosphorylase a
			Phosphorylase Kinase Is Activated by Phosphorylation and Calcium Ions
			An Isozymic Form of Glycogen Phosphorylase Exists in the Brain
		24.3 Epinephrine and Glucagon Signal the Need for Glycogen Breakdown
			G Proteins Transmit the Signal for the Initiation of Glycogen Breakdown
			Glycogen Breakdown Must Be Rapidly Turned Off When Necessary
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 25 Glycogen Synthesis
		25.1 Glycogen Is Synthesized and Degraded by Different Pathways
			UDP-Glucose Is an Activated Form of Glucose
			Glycogen Synthase Catalyzes the Transfer of Glucose from UDP-Glucose to a Growing Chain
			A Branching Enzyme Forms Alpha-1,6 Linkages
			Glycogen Synthase Is the Key Regulatory Enzyme in Glycogen Synthesis
			Glycogen Is an Efficient Storage Form of Glucose
		25.2 Metabolism in Context: Glycogen Breakdown and Synthesis Are Reciprocally Regulated
			Protein Phosphatase 1 Reverses the Regulatory Effects of Kinases on Glycogen Metabolism
			Insulin Stimulates Glycogen Synthesis by Inactivating Glycogen Synthase Kinase
			Glycogen Metabolism in the Liver Regulates the Blood-Glucose Concentration
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 26 The Pentose Phosphate Pathway
		26.1 The Pentose Phosphate Pathway Yields NADPH and Five-Carbon Sugars
			Two Molecules of NADPH Are Generated in the Conversion of Glucose 6-Phosphate into Ribulose 5-Phosphate
			The Pentose Phosphate Pathway and Glycolysis Are Linked by Transketolase and Transaldolase
		26.2 Metabolism in Context: Glycolysis and the Pentose Phosphate Pathway Are Coordinately Controlled
			The Rate of the Oxidative Phase of the Pentose Phosphate Pathway Is Controlled by the Concentration of NADP+
			The Fate of Glucose 6-Phosphate Depends on the Need for NADPH, Ribose 5-Phosphate, and ATP
				Mode 1
				Mode 2
				Mode 3
				Mode 4
		26.3 Glucose 6-Phosphate Dehydrogenase Lessens Oxidative Stress
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
Section 12 Fatty Acid and Lipid Metabolism
	Chapter 27 Fatty Acid Degradation
		27.1 Fatty Acids Are Processed in Three Stages
			Free Fatty Acids and Glycerol Are Released into the Blood
			Fatty Acids Are Linked to Coenzyme A Before They Are Oxidized
			Acetyl CoA, NADH, and FADH 2 Are Generated by Fatty Acid Oxidation
			The Complete Oxidation of Palmitate Yields 106 Molecules of ATP
		27.2 The Degradation of Unsaturated and Odd-Chain Fatty Acids Requires Additional Steps
			An Isomerase and a Reductase Are Required for the Oxidation of Unsaturated Fatty Acids
			Odd-Chain Fatty Acids Yield Propionyl CoA in the Final Thiolysis Step
		27.3 Ketone Bodies Are Another Fuel Source Derived from Fats
			Ketone-Body Synthesis Takes Place in the Liver
			Animals Cannot Convert Fatty Acids into Glucose
		27.4 Metabolism in Context: Fatty Acid Metabolism Is a Source of Insight into Various Physiological States
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 28 Fatty Acid Synthesis
		28.1 Fatty Acid Synthesis Takes Place in Three Stages
			Citrate Carries Acetyl Groups from Mitochondria to the Cytoplasm
			Several Sources Supply NADPH for Fatty Acid Synthesis
			The Formation of Malonyl CoA Is the Committed Step in Fatty Acid Synthesis
			Fatty Acid Synthesis Consists of a Series of Condensation, Reduction, Dehydration, and Reduction Reactions
			The Synthesis of Palmitate Requires Eight Molecules of Acetyl CoA, 14 Molecules of NADPH, and Seven Molecules of ATP
			Fatty Acids Are Synthesized by a Multifunctional Enzyme Complex in Animals
		28.2 Additional Enzymes Elongate and Desaturate Fatty Acids
			Membrane-Bound Enzymes Generate Unsaturated Fatty Acids
			Eicosanoid Hormones Are Derived from Polyunsaturated Fatty Acids
		28.3 Acetyl CoA Carboxylase Is a Key Regulator of Fatty Acid Metabolism
			Acetyl CoA Carboxylase Is Regulated by Conditions in the Cell
			Acetyl CoA Carboxylase Is Regulated by a Variety of Hormones
				Regulation by glucagon and epinephrine
				Regulation by insulin
				Response to diet
			AMP-Activated Protein Kinase Is a Key Regulator of Metabolism
		28.4 Metabolism in Context: Ethanol Alters Energy Metabolism in the Liver
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 29 Lipid Synthesis: Storage Lipids, Phospholipids, and Cholesterol
		29.1 Phosphatidate Is a Precursor of Storage Lipids and Many Membrane Lipids
			Triacylglycerol Is Synthesized from Phosphatidate in Two Steps
			Phospholipid Synthesis Requires Activated Precursors
				Synthesis from an activated diacylglycerol
				Synthesis from an activated alcohol
			Sphingolipids Are Synthesized from Ceramide
			Phosphatidic Acid Phosphatase Is a Key Regulatory Enzyme in Lipid Metabolism
		29.2 Cholesterol Is Synthesized from Acetyl Coenzyme A in Three Stages
			The Synthesis of Mevalonate Initiates the Synthesis of Cholesterol
			Squalene (C30) Is Synthesized from Six Molecules of Isopentenyl Pyrophosphate (C5)
			Squalene Cyclizes to Form Cholesterol
		29.3 The Regulation of Cholesterol Synthesis Takes Place at Several Levels
		29.4 Lipoproteins Transport Cholesterol and Triacylglycerols Throughout the Organism
			Low-Density Lipoproteins Play a Central Role in Cholesterol Metabolism
		29.5 Important Biochemicals Are Synthesized from Cholesterol and Isoprene
			Steroid Hormones Are Crucial Signal Molecules
			Vitamin D Is Derived from Cholesterol by the Energy of Sunlight
			Oxygen Atoms Are Added to Steroids by Cytochrome P450 Monooxygenases
			Metabolism in Context: Ethanol Also Is Processed by the Cytochrome P450 System
			Five-Carbon Units Are Joined to Form a Wide Variety of Biomolecules
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 13 The Metabolism of Nitrogen-Containing Molecules
	Chapter 30 Amino Acid Degradation and the Urea Cycle
		30.1 Nitrogen Removal Is the First Step in the Degradation of Amino Acids
			Alpha-Amino Groups Are Converted into Ammonium Ions by the Oxidative Deamination of Glutamate
			Serine and Threonine Can Be Directly Deaminated
			Peripheral Tissues Transport Nitrogen to the Liver
		30.2 Ammonium Ion Is Converted into Urea in Most Terrestrial Vertebrates
			Carbamoyl Phosphate Synthetase Is the Key Regulatory Enzyme for Urea Synthesis
			Carbamoyl Phosphate Reacts with Ornithine to Begin the Urea Cycle
			The Urea Cycle Is Linked to Gluconeogenesis
		30.3 Carbon Atoms of Degraded Amino Acids Emerge as Major Metabolic Intermediates
			Pyruvate Is a Point of Entry into Metabolism
			Oxaloacetate Is Another Point of Entry into Metabolism
			Alpha-Ketoglutarate Is Yet Another Point of Entry into Metabolism
			Succinyl Coenzyme A Is a Point of Entry for Several Amino Acids
			Threonine Deaminase Initiates the Degradation of Threonine
			Methionine Is Degraded into Succinyl Coenzyme A
			The Branched-Chain Amino Acids Yield Acetyl Coenzyme A, Acetoacetate, or Succinyl Coenzyme A
			Oxygenases Are Required for the Degradation of Aromatic Amino Acids
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 31 Amino Acid Synthesis
		31.1 The Nitrogenase Complex Fixes Nitrogen
			The Molybdenum–Iron Cofactor of Nitrogenase Binds and Reduces Atmospheric Nitrogen
			Ammonium Ion Is Incorporated into an Amino Acid Through Glutamate and Glutamine
		31.2 Amino Acids Are Made from Intermediates of Major Pathways
			Human Beings Can Synthesize Some Amino Acids but Must Obtain Others from the Diet
			Some Amino Acids Can Be Made by Simple Transamination Reactions
			Serine, Cysteine, and Glycine Are Formed from 3-Phosphoglycerate
			S-Adenosylmethionine Is the Major Donor of Methyl Groups
		31.3 Feedback Inhibition Regulates Amino Acid Biosynthesis
			The Committed Step Is the Common Site of Regulation
			Branched Pathways Require Sophisticated Regulation
				Feedback inhibition and activation
				Enzyme multiplicity
				Cumulative feedback inhibition
		31.4 Amino Acids Are Precursors of Many Biomolecules
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 32 Nucleotide Metabolism
		32.1 An Overview of Nucleotide Biosynthesis and Nomenclature
		32.2 The Pyrimidine Ring Is Assembled and Then Attached to a Ribose Sugar
			CTP Is Formed by the Amination of UTP
			Kinases Convert Nucleoside Monophosphates into Nucleoside Triphosphates
		32.3 The Purine Ring Is Assembled on Ribose Phosphate
			AMP and GMP Are Formed from IMP
			Bases Can Be Recycled by Salvage Pathways
		32.4 Ribonucleotides Are Reduced to Deoxyribonucleotides
			Thymidylate Is Formed by the Methylation of Deoxyuridylate
		32.5 Nucleotide Biosynthesis Is Regulated by Feedback Inhibition
			Pyrimidine Biosynthesis Is Regulated by Aspartate Transcarbamoylase
			The Synthesis of Purine Nucleotides Is Controlled by Feedback Inhibition at Several Sites
		32.6 Disruptions in Nucleotide Metabolism Can Cause Pathological Conditions
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 14 Nucleic Acid Structure and DNA Replication
	Chapter 33 The Structure of Informational Macromolecules: DNA and RNA
		33.1 A Nucleic Acid Consists of Bases Linked to a Sugar–Phosphate Backbone
			DNA and RNA Differ in the Sugar Component and One of the Bases
			Nucleotides Are the Monomeric Units of Nucleic Acids
			DNA Molecules Are Very Long and Have Directionality
		33.2 Nucleic Acid Strands Can Form a Double-Helical Structure
			The Double Helix Is Stabilized by Hydrogen Bonds and the Hydrophobic Effect
			The Double Helix Facilitates the Accurate Transmission of Hereditary Information
			Meselson and Stahl Demonstrated That Replication Is Semiconservative
			The Strands of the Double Helix Can Be Reversibly Separated
		33.3 DNA Double Helices Can Adopt Multiple Forms
			Z-DNA Is a Left-Handed Double Helix in Which Backbone Phosphoryl Groups Zigzag
			The Major and Minor Grooves Are Lined by Sequence-Specific Hydrogen-Bonding Groups
			Double-Stranded DNA Can Wrap Around Itself to Form Supercoiled Structures
		33.4 Eukaryotic DNA Is Associated with Specific Proteins
			Nucleosomes Are Complexes of DNA and Histones
			Eukaryotic DNA Is Wrapped Around Histones to Form Nucleosomes
		33.5 RNA Can Adopt Elaborate Structures
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 34 DNA Replication
		34.1 DNA Is Replicated by Polymerases
			DNA Polymerase Catalyzes Phosphodiester-Linkage Formation
			The Specificity of Replication Is Dictated by the Complementarity of Bases
			Topoisomerases Prepare the Double Helix for Unwinding
			Many Polymerases Proofread the Newly Added Bases and Excise Errors
		34.2 DNA Replication Is Highly Coordinated
			DNA Replication in E. coli Begins at a Unique Site
			An RNA Primer Synthesized by Primase Enables DNA Synthesis to Begin
			One Strand of DNA Is Made Continuously and the Other Strand Is Synthesized in Fragments
			DNA Replication Requires Highly Processive Polymerases
			The Leading and Lagging Strands Are Synthesized in a Coordinated Fashion
			DNA Replication Is Terminated at Distinct Sites in E. Coli
			DNA Synthesis Is More Complex in Eukaryotes Than in Bacteria
			Telomeres Are Unique Structures at the Ends of Linear Chromosomes
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 35 DNA Repair and Recombination
		35.1 Errors Can Arise in DNA Replication
			Bases Can Be Damaged by Oxidizing Agents, Alkylating Agents, and Light
		35.2 DNA Damage Can Be Detected and Repaired
			The Presence of Thymine Instead of Uracil in DNA Permits the Repair of Deaminated Cytosine
		35.3 DNA Recombination Plays Important Roles in Replication and Repair
			Double-Strand Breaks Can Be Repaired by Recombination
			DNA Recombination Is Important in a Variety of Biological Processes
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
Section 15 RNA Synthesis, Processing, and Regulation
	Chapter 36 RNA Synthesis and Regulation in Bacteria
		36.1 Cellular RNA Is Synthesized by RNA Polymerases
			Genes Are the Transcriptional Units
			RNA Polymerase Is Composed of Multiple Subunits
		36.2 RNA Synthesis Comprises Three Stages
			Transcription Is Initiated at Promoter Sites on the DNA Template
			Sigma Subunits of RNA Polymerase Recognize Promoter Sites
			RNA Strands Grow in the 5′-to-3′ Direction
			Elongation Takes Place at Transcription Bubbles That Move Along the DNA Template
			An RNA Hairpin Followed by Several Uracil Residues Terminates the Transcription of Some Genes
			The Rho Protein Helps Terminate the Transcription of Some Genes
			Precursors of Transfer and Ribosomal RNA Are Cleaved and Chemically Modified After Transcription
		36.3 The lac Operon Illustrates the Control of Bacterial Gene Expression
			An Operon Consists of Regulatory Elements and Protein-Encoding Genes
			Ligand Binding Can Induce Structural Changes in Regulatory Proteins
			Transcription Can Be Stimulated by Proteins That Contact RNA Polymerase
			Some Messenger RNAs Directly Sense Metabolite Concentrations
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 37 Gene Expression in Eukaryotes
		37.1 Eukaryotic Cells Have Three Types of RNA Polymerases
		37.2 RNA Polymerase II Requires Complex Regulation
			The Transcription Factor IID Protein Complex Initiates the Assembly of the Active Transcription Complex
			Enhancer Sequences Can Stimulate Transcription at Start Sites Thousands of Bases Away
			Multiple Transcription Factors Interact with Eukaryotic Promoters and Enhancers
		37.3 Gene Expression Is Regulated by Hormones
			Nuclear Hormone Receptors Have Similar Domain Structures
			Nuclear Hormone Receptors Recruit Coactivators and Corepressors
		37.4 Histone Acetylation Results in Chromatin Remodeling
			Metabolism in Context: Acetyl CoA Plays a Key Role in the Regulation of Transcription
			Histone Deacetylases Contribute to Transcriptional Repression
			The Methylation of DNA Can Alter Patterns of Gene Expression
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 38 RNA Processing in Eukaryotes
		38.1 Mature Ribosomal RNA Is Generated by the Cleavage of a Precursor Molecule
		38.2 Transfer RNA Is Extensively Processed
		38.3 Messenger RNA Is Modified and Spliced
			Sequences at the Ends of Introns Specify Splice Sites in mRNA Precursors
			Small Nuclear RNAs in Spliceosomes Catalyze the Splicing of mRNA Precursors
			The Transcription and Processing of mRNA Are Coupled
		38.4 RNA Can Function as a Catalyst
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
Section 16 Protein Synthesis and Recombinant DNA Techniques
	Chapter 39 The Genetic Code
		39.1 The Genetic Code Links Nucleic Acid and Protein Information
			The Genetic Code Is Nearly Universal
			Transfer RNA Molecules Have a Common Design
			Some Transfer RNA Molecules Recognize More Than One Codon Because of Wobble in Base-Pairing
			The Synthesis of Long Proteins Requires a Low Error Frequency
		39.2 Amino Acids Are Activated by Attachment to Transfer RNA
			Amino Acids Are First Activated by Adenylation
			Aminoacyl-tRNA Synthetases Have Highly Discriminating Amino Acid Activation Sites
			Proofreading by Aminoacyl-tRNA Synthetases Increases the Fidelity of Protein Synthesis
			Synthetases Recognize the Anticodon Loops and Acceptor Stems of Transfer RNA Molecules
		39.3 A Ribosome Is a Ribonucleoprotein Particle Made of Two Subunits
			Ribosomal RNAs Play a Central Role in Protein Synthesis
			Messenger RNA Is Translated in the 5′-to-3′ Direction
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 40 The Mechanism of Protein Synthesis
		40.1 Protein Synthesis Decodes the Information in Messenger RNA
			Ribosomes Have Three tRNA-Binding Sites That Bridge the 30S and 50S Subunits
			The Start Signal Is AUG Preceded by Several Bases That Pair with 16S Ribosomal RNA
			Bacterial Protein Synthesis Is Initiated by Formylmethionyl Transfer RNA
			Formylmethionyl-tRNAf Is Placed in the P Site of the Ribosome in the Formation of the 70S Initiation Complex
			Elongation Factors Deliver Aminoacyl-tRNA to the Ribosome
		40.2 Peptidyl Transferase Catalyzes Peptide-Bond Synthesis
			The Formation of a Peptide Bond Is Followed by the GTP-Driven Translocation of tRNAs and mRNA
			Protein Synthesis Is Terminated by Release Factors That Read Stop Codons
		40.3 Bacteria and Eukaryotes Differ in the Initiation of Protein Synthesis
		40.4 A Variety of Biomolecules Can Inhibit Protein Synthesis
		40.5 Ribosomes Bound to the Endoplasmic Reticulum Manufacture Secretory and Membrane Proteins
			Protein Synthesis Begins on Ribosomes That Are Free in the Cytoplasm
			Signal Sequences Mark Proteins for Translocation Across the Endoplasmic Reticulum Membrane
		40.6 Protein Synthesis Is Regulated by a Number of Mechanisms
			Messenger RNA Use Is Subject to Regulation
			The Stability of Messenger RNA Also Can Be Regulated
			Small RNAs Can Regulate mRNA Stability and Use
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answers to Quick Quizzes
		Problems
	Chapter 41 Recombinant DNA Techniques
		41.1 Nucleic Acids Can Be Synthesized from Protein-Sequence Data
			Protein Sequence Is a Guide to Nucleic Acid Information
			DNA Probes Can Be Synthesized by Automated Methods
		41.2 Recombinant DNA Technology Has Revolutionized All Aspects of Biology
			Restriction Enzymes Split DNA into Specific Fragments
			Restriction Fragments Can Be Separated by Gel Electrophoresis and Visualized
			Restriction Enzymes and DNA Ligase Are Key Tools for Forming Recombinant DNA Molecules
		41.3 Eukaryotic Genes Can Be Expressed in Bacteria
			Complementary DNA Prepared from mRNA Can Be Expressed in Host Cells
			Estrogen-Receptor cDNA Can Be Identified by Screening a cDNA Library
			Complementary DNA Libraries Can Be Screened for Synthesized Protein
			Specific Genes Can Be Cloned from Digests of Genomic DNA
			DNA Can Be Sequenced by the Controlled Termination of Replication
			Selected DNA Sequences Can Be Greatly Amplified by the Polymerase Chain Reaction
		41.4 Eukaryotic Genes Can Be Quantitated and Manipulated with Considerable Precision
			Gene-Expression Levels Can Be Comprehensively Examined
			New Genes Inserted into Eukaryotic Cells Can Be Efficiently Expressed
			Transgenic Animals Harbor and Express Genes Introduced into Their Germ Lines
			Gene Disruption and Genome Editing Provide Clues to Gene Function and Opportunities for New Therapies
		Summary
		Appendix: Biochemistry in Focus
		Appendix: Problem-Solving Strategies
		Key Terms
		Answer to Quick Quiz
		Problems
Appendix A: Physical Constants and Conversion of Units
Appendix B: Acidity Constants
Appendix C: Standard Bond Lengths
Appendix D: Water-Soluble Vitamins
Glossary
Answers to Problems
Index
Common Abbreviations in Biochemistry
Selected Readings
Inside Back Cover
Back Cover