Essential Cell Biology 5th edition

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xviContentsCHAPTER 2Chemical Components of Cells 39CHEMICAL BONDS 40Cells Are Made of Relatively Few Types of Atoms 40The Outermost Electrons Determine How Atoms Interact 41Covalent Bonds Form by the Sharing of Electrons 43Some Covalent Bonds Involve More Than One Electron Pair 44Electrons in Covalent Bonds Are Often Shared Unequally 45Covalent Bonds Are Strong Enough to Survive the Conditions Inside Cells 45Ionic Bonds Form by the Gain and Loss of Electrons 46Hydrogen Bonds Are Important Noncovalent Bonds for Many Biological Molecules 47Four Types of Weak Interactions Help Bring Molecules Together in Cells 47Some Polar Molecules Form Acids and Bases in Water 49SMALL MOLECULES IN CELLS 50A Cell Is Formed from Carbon Compounds 50Cells Contain Four Major Families of Small Organic Molecules 51Sugars Are both Energy Sources and Subunits of Polysaccharides 52Fatty Acid Chains Are Components of Cell Membranes 54Amino Acids Are the Subunits of Proteins 56Nucleotides Are the Subunits of DNA and RNA 56MACROMOLECULES IN CELLS 58Each Macromolecule Contains a Specific Sequence of Subunits 59Noncovalent Bonds Specify the Precise Shape of a Macromolecule 62Noncovalent Bonds Allow a Macromolecule to Bind Other Selected Molecules 62ESSENTIAL CONCEPTS 64QUESTIONS 65CHAPTER 3Energy, Catalysis, and Biosynthesis 81THE USE OF ENERGY BY CELLS 82Biological Order Is Made Possible by the Release of Heat Energy from Cells 83Cells Can Convert Energy from One Form to Another 84Photosynthetic Organisms Use Sunlight to Synthesize Organic Molecules 85Cells Obtain Energy by the Oxidation of Organic Molecules 86Oxidation and Reduction Involve Electron Transfers 87FREE ENERGY AND CATALYSIS 88Chemical Reactions Proceed in the Direction That Causes a Loss of Free Energy 89Enzymes Reduce the Energy Needed to Initiate Spontaneous Reactions 89The Free-Energy Change for a Reaction Determines Whether It Can Occur 90G Changes as a Reaction Proceeds Toward Equilibrium 92The Standard Free-Energy Change, G°, Makes It Possible to Compare the Energetics ofDifferent Reactions 92The Equilibrium Constant Is Directly Proportional to G° 96In Complex Reactions, the Equilibrium Constant Includes the Concentrations ofAll Reactants and Products 96

ContentsxviiThe Equilibrium Constant Also Indicates the Strength of Noncovalent Binding Interactions 97For Sequential Reactions, the Changes in Free Energy Are Additive 98Enzyme-catalyzed Reactions Depend on Rapid Molecular Collisions 99Noncovalent Interactions Allow Enzymes to Bind Specific Molecules 100ACTIVATED CARRIERS AND BIOSYNTHESIS 101The Formation of an Activated Carrier Is Coupled to an Energetically Favorable Reaction 101ATP Is the Most Widely Used Activated Carrier 104Energy Stored in ATP Is Often Harnessed to Join Two Molecules Together 106NADH and NADPH Are Both Activated Carriers of Electrons 106NADPH and NADH Have Different Roles in Cells 108Cells Make Use of Many Other Activated Carriers 108The Synthesis of Biological Polymers Requires an Energy Input 110ESSENTIAL CONCEPTS 113QUESTIONS 114CHAPTER 4Protein Structure and Function 117THE SHAPE AND STRUCTURE OF PROTEINS 119The Shape of a Protein Is Specified by Its Amino Acid Sequence 119Proteins Fold into a Conformation of Lowest Energy 122Proteins Come in a Wide Variety of Complicated Shapes 124The a Helix and the b Sheet Are Common Folding Patterns 126Helices Form Readily in Biological Structures 127b Sheets Form Rigid Structures at the Core of Many Proteins 129Misfolded Proteins Can Form Amyloid Structures That Cause Disease 129Proteins Have Several Levels of Organization 129Proteins Also Contain Unstructured Regions 130Few of the Many Possible Polypeptide Chains Will Be Useful 131Proteins Can Be Classified into Families 132Large Protein Molecules Often Contain More than One Polypeptide Chain 132Proteins Can Assemble into Filaments, Sheets, or Spheres 134Some Types of Proteins Have Elongated Fibrous Shapes 134Extracellular Proteins Are Often Stabilized by Covalent Cross-Linkages 135HOW PROTEINS WORK 137All Proteins Bind to Other Molecules 137Humans Produce Billions of Different Antibodies, Each with a Different Binding Site 138Enzymes Are Powerful and Highly Specific Catalysts 139Enzymes Greatly Accelerate the Speed of Chemical Reactions 142Lysozyme Illustrates How an Enzyme Works 143Many Drugs Inhibit Enzymes 147Tightly Bound Small Molecules Add Extra Functions to Proteins 148HOW PROTEINS ARE CONTROLLED 149The Catalytic Activities of Enzymes Are Often Regulated by Other Molecules 150Allosteric Enzymes Have Two or More Binding Sites That Influence One Another 151Phosphorylation Can Control Protein Activity by Causing a Conformational Change 152Covalent Modifications Also Control the Location and Interaction of Proteins 153Regulatory GTP-Binding Proteins Are Switched On and Off by the Gain and Loss of a Phosphate Group 154

Contents

xvii

The Equilibrium Constant Also Indicates the Strength of Noncovalent Binding Interactions 97

For Sequential Reactions, the Changes in Free Energy Are Additive 98

Enzyme-catalyzed Reactions Depend on Rapid Molecular Collisions 99

Noncovalent Interactions Allow Enzymes to Bind Specific Molecules 100

ACTIVATED CARRIERS AND BIOSYNTHESIS 101

The Formation of an Activated Carrier Is Coupled to an Energetically Favorable Reaction 101

ATP Is the Most Widely Used Activated Carrier 104

Energy Stored in ATP Is Often Harnessed to Join Two Molecules Together 106

NADH and NADPH Are Both Activated Carriers of Electrons 106

NADPH and NADH Have Different Roles in Cells 108

Cells Make Use of Many Other Activated Carriers 108

The Synthesis of Biological Polymers Requires an Energy Input 110

ESSENTIAL CONCEPTS 113

QUESTIONS 114

CHAPTER 4

Protein Structure and Function 117

THE SHAPE AND STRUCTURE OF PROTEINS 119

The Shape of a Protein Is Specified by Its Amino Acid Sequence 119

Proteins Fold into a Conformation of Lowest Energy 122

Proteins Come in a Wide Variety of Complicated Shapes 124

The a Helix and the b Sheet Are Common Folding Patterns 126

Helices Form Readily in Biological Structures 127

b Sheets Form Rigid Structures at the Core of Many Proteins 129

Misfolded Proteins Can Form Amyloid Structures That Cause Disease 129

Proteins Have Several Levels of Organization 129

Proteins Also Contain Unstructured Regions 130

Few of the Many Possible Polypeptide Chains Will Be Useful 131

Proteins Can Be Classified into Families 132

Large Protein Molecules Often Contain More than One Polypeptide Chain 132

Proteins Can Assemble into Filaments, Sheets, or Spheres 134

Some Types of Proteins Have Elongated Fibrous Shapes 134

Extracellular Proteins Are Often Stabilized by Covalent Cross-Linkages 135

HOW PROTEINS WORK 137

All Proteins Bind to Other Molecules 137

Humans Produce Billions of Different Antibodies, Each with a Different Binding Site 138

Enzymes Are Powerful and Highly Specific Catalysts 139

Enzymes Greatly Accelerate the Speed of Chemical Reactions 142

Lysozyme Illustrates How an Enzyme Works 143

Many Drugs Inhibit Enzymes 147

Tightly Bound Small Molecules Add Extra Functions to Proteins 148

HOW PROTEINS ARE CONTROLLED 149

The Catalytic Activities of Enzymes Are Often Regulated by Other Molecules 150

Allosteric Enzymes Have Two or More Binding Sites That Influence One Another 151

Phosphorylation Can Control Protein Activity by Causing a Conformational Change 152

Covalent Modifications Also Control the Location and Interaction of Proteins 153

Regulatory GTP-Binding Proteins Are Switched On and Off by the Gain and Loss of a Phosphate Group 154

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