| Preface |
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xi | |
| Part 1 Foundations |
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1 The Chemical Basis of Life |
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1 | (23) |
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1.1 What Is Biochemistry? |
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1 | (2) |
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3 | (4) |
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Cells contain four major types of biomolecules |
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3 | (3) |
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There are three major kinds of biological polymers |
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6 | (1) |
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Box 1.A Units Used in Biochemistry |
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7 | (3) |
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1.3 Energy and Metabolism |
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10 | (4) |
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Enthalpy and entropy are components of free energy |
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10 | (1) |
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ΔG is less than zero for a spontaneous process |
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11 | (1) |
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Life is thermodynamically possible |
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12 | (2) |
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1.4 The Origin and Evolution of Life |
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14 | (3) |
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14 | (2) |
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16 | (1) |
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Box 1.13 How Does Evolution Work? |
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17 | (7) |
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24 | (28) |
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2.1 Water Molecules and Hydrogen Bonds |
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24 | (4) |
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Hydrogen bonds are one type of electrostatic force |
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26 | (2) |
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Box 2.A Why Do Some Drugs Contain Fluorine? |
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28 | (1) |
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Water dissolves many compounds |
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28 | (1) |
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2.2 The Hydrophobic Effect |
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29 | (3) |
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Amphiphilic molecules experience both hydrophilic interactions and the hydrophobic effect |
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31 | (1) |
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The hydrophobic core of a lipid bilayer is a barrier to diffusion |
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31 | (1) |
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Box 2.B Sweat, Exercise, and Sports Drinks |
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32 | (1) |
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33 | (2) |
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[ H+] and [ OH-] are inversely related |
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33 | (1) |
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The pH of a solution can be altered |
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34 | (1) |
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Box 2.0 Atmospheric CO2 and Ocean Acidification |
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35 | (5) |
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A pK value describes an acid's tendency to ionize |
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36 | (1) |
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The pH of a solution of acid is related to the pK |
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37 | (3) |
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2.4 Tools and Techniques: Buffers |
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40 | (2) |
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2.5 Clinical Connection: Acid-Base Balance in Humans |
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42 | (10) |
| Part 2 Molecular Structure and Function |
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52 | (33) |
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52 | (4) |
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Nucleic acids are polymers of nucleotides |
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53 | (1) |
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Some nucleotides have other functions |
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54 | (2) |
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3.2 Nucleic Acid Structure |
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56 | (5) |
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56 | (3) |
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59 | (1) |
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Nucleic acids can be denatured and renatured |
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59 | (2) |
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61 | (3) |
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62 | (1) |
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A mutated gene can cause disease |
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63 | (1) |
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64 | (4) |
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Gene number is roughly correlated with organismal complexity |
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65 | (1) |
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Genes are identified by comparing sequences |
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66 | (1) |
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Genomic data reveal biological functions |
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67 | (1) |
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3.5 Tools and Techniques: Manipulating DNA |
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68 | (4) |
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Cutting and pasting generates recombinant DNA |
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69 | (2) |
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The polymerase chain reaction amplifies DNA |
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71 | (1) |
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Box 3.A Genetically Modified Organisms |
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72 | (2) |
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Box 3.B DNA Fingerprinting |
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74 | (11) |
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DNA sequencing uses DNA polymerase to make a complementary strand |
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74 | (2) |
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76 | (9) |
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85 | (34) |
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4.1 Amino Acids, the Building Blocks of Proteins |
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86 | (2) |
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The 20 amino acids have different chemical properties |
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87 | (1) |
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Box 4.A Does Chirality Matter? |
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88 | (2) |
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Box 4.B Monosodium Glutamate |
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90 | (4) |
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Peptide bonds link amino acids in proteins |
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90 | (3) |
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The amino acid sequence is the first level of protein structure |
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93 | (1) |
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4.2 Secondary Structure: The Conformation of the Peptide Group |
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94 | (3) |
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The a helix exhibits a twisted backbone conformation |
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95 | (1) |
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The p sheet contains multiple polypeptide strands |
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95 | (1) |
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Proteins also contain irregular secondary structure |
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96 | (1) |
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4.3 Tertiary Structure and Protein Stability |
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97 | (7) |
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Proteins have hydrophobic cores |
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98 | (1) |
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Protein structures are stabilized mainly by the hydrophobic effect |
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99 | (1) |
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Other interactions help stabilize proteins |
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100 | (1) |
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Protein folding begins with the formation of secondary structures |
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101 | (1) |
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Some proteins have more than one conformation |
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102 | (2) |
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104 | (1) |
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4.5 Clinical Connection: Protein Misfolding and Disease |
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105 | (2) |
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4.6 Tools and Techniques: Analyzing Protein Structure |
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107 | (3) |
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Chromatography takes advantage of a polypeptide's unique properties |
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107 | (2) |
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Mass spectrometry reveals amino acid sequences |
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109 | (1) |
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Protein structures are determined by X-ray crystallography, electron crystallography, and NMR spectroscopy |
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110 | (1) |
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Box 4.0 Mass Spectrometry Applications |
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110 | (9) |
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119 | (35) |
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5.1 Myoglobin and Hemoglobin: Oxygen-Binding Proteins |
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120 | (4) |
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Oxygen binding to myoglobin depends on the oxygen concentration |
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120 | (1) |
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Myoglobin and hemoglobin are related by evolution |
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121 | (2) |
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Oxygen binds cooperatively to hemoglobin |
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123 | (1) |
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A conformational shift explains hemoglobin's cooperative behavior |
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124 | (1) |
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Box 5.A Carbon Monoxide Poisoning |
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124 | (3) |
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H+ ions and bisphosphoglycerate regulate oxygen binding to hemoglobin in vivo |
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126 | (1) |
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5.2 Clinical Connection: Hemoglobin Variants |
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127 | (3) |
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130 | (7) |
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Actin filaments are most abundant |
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130 | (1) |
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Actin filaments continuously extend and retract |
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131 | (1) |
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Tubulin forms hollow microtubules |
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132 | (2) |
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Some drugs affect microtubules |
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134 | (1) |
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Keratin is an intermediate filament |
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135 | (1) |
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Collagen is a triple helix |
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136 | (1) |
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Box 5.B Vitamin C Deficiency Causes Scurvy |
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137 | (2) |
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Collagen molecules are covalently cross-linked |
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139 | (1) |
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Box 5.0 Bone and Collagen Defects |
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139 | (2) |
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141 | (3) |
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Myosin has two heads and a long tail |
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141 | (1) |
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Myosin operates through a lever mechanism |
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142 | (1) |
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Kinesin is a microtubule-associated motor protein |
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143 | (1) |
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Box 5.D Myosin Mutations and Deafness |
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144 | (10) |
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Kinesin is a processive motor |
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146 | (8) |
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154 | (29) |
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154 | (4) |
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Enzymes are usually named after the reaction they catalyze |
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157 | (1) |
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6.2 Chemical Catalytic Mechanisms |
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158 | (4) |
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A catalyst provides a reaction pathway with a lower activation energy barrier |
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159 | (1) |
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Enzymes use chemical catalytic mechanisms |
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160 | (2) |
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Box 6.A Depicting Reaction Mechanisms |
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162 | (4) |
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The catalytic triad of chymotrypsin promotes peptide bond hydrolysis |
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164 | (2) |
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6.3 Unique Properties of Enzyme Catalysts |
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166 | (3) |
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Enzymes stabilize the transition state |
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166 | (2) |
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Efficient catalysis depends on proximity and orientation effects |
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168 | (1) |
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The active-site microenvironment promotes catalysis |
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168 | (1) |
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6.4 Chymotrypsin in Context |
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169 | (4) |
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Not all serine proteases are related by evolution |
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170 | (1) |
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Enzymes with similar mechanisms exhibit different substrate specificity |
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170 | (1) |
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Chymotrypsin is activated by proteolysis |
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171 | (1) |
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Protease inhibitors limit protease activity |
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172 | (1) |
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6.5 Clinical Connection: Blood Coagulation |
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173 | (10) |
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7 Enzyme Kinetics and Inhibition |
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183 | (32) |
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7.1 Introduction to Enzyme Kinetics |
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183 | (3) |
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7.2 Derivation and Meaning of the Michaelis-Menten Equation |
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186 | (8) |
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Rate equations describe chemical processes |
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186 | (1) |
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The Michaelis-Menten equation is a rate equation for an enzyme-catalyzed reaction |
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187 | (2) |
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KM is the substrate concentration at which velocity is half-maximal |
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189 | (1) |
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The catalytic constant describes how quickly an enzyme can act |
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190 | (1) |
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kcat/KM indicates catalytic efficiency |
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190 | (1) |
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KM and Vmax are experimentally determined |
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191 | (1) |
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Not all enzymes fit the simple Michaelis-Menten model |
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192 | (2) |
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194 | (4) |
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Some inhibitors act irreversibly |
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195 | (1) |
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Competitive inhibition is the most common form of reversible enzyme inhibition |
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195 | (2) |
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Transition state analogs inhibit enzymes |
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197 | (1) |
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Box 7.A Inhibitors of HIV Protease |
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198 | (6) |
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Other types of inhibitors affect Vmax |
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199 | (1) |
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Allosteric enzyme regulation includes inhibition and activation |
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200 | (3) |
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Several factors may influence enzyme activity |
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203 | (1) |
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7.4 Clinical Connection: Drug Development |
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204 | (11) |
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215 | (20) |
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215 | (1) |
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Fatty acids contain long hydrocarbon chains |
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216 | (1) |
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Box 8.A Omega-3 Fatty Acids |
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216 | (5) |
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Some lipids contain polar head groups |
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217 | (2) |
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Lipids perform a variety of physiological functions |
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219 | (2) |
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Box 8.B The Lipid Vitamins A, D, E, and K |
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221 | (1) |
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222 | (3) |
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The bilayer is a fluid structure |
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223 | (1) |
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Natural bilayers are asymmetric |
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224 | (1) |
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225 | (3) |
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Integral membrane proteins span the bilayer |
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225 | (1) |
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An a helix can cross the bilayer |
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226 | (1) |
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A transmembrane β sheet forms a barrel |
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226 | (1) |
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Lipid-linked proteins are anchored in the membrane |
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227 | (1) |
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8.4 The Fluid Mosaic Model |
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228 | (7) |
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Membrane glycoproteins face the cell exterior |
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229 | (6) |
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235 | (25) |
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9.1 The Thermodynamics of Membrane Transport |
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235 | (5) |
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Ion movements alter membrane potential |
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237 | (1) |
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Membrane proteins mediate transmembrane ion movement |
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237 | (3) |
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240 | (2) |
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Porins are β barrel proteins |
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240 | (1) |
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Ion channels are highly selective |
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241 | (1) |
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242 | (3) |
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Gated channels undergo conformational changes |
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242 | (1) |
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Aquaporins are water-specific pores |
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243 | (1) |
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Some transport proteins alternate between conformations |
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244 | (1) |
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245 | (3) |
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The Na,K-ATPase changes conformation as it pumps ions across the membrane |
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246 | (1) |
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ABC transporters mediate drug resistance |
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247 | (1) |
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Secondary active transport exploits existing gradients |
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247 | (1) |
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248 | (2) |
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Box 9.B Antidepressants Block Serotonin Transport |
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250 | (3) |
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SNARES link vesicle and plasma membranes |
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251 | (1) |
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Endocytosis is the reverse of exocytosis |
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252 | (1) |
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253 | (7) |
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260 | (23) |
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10.1 General Features of Signaling Pathways |
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260 | (2) |
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A ligand binds to a receptor with a characteristic affinity |
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261 | (1) |
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Box 10.A Bacterial Quorum Sensing |
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262 | (3) |
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Most signaling occurs through two types of receptors |
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263 | (1) |
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The effects of signaling are limited |
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264 | (1) |
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10.2 G Protein Signaling Pathways |
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265 | (5) |
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G protein-coupled receptors include seven transmembrane helices |
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265 | (1) |
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The receptor activates a G protein |
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265 | (1) |
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Adenylate cyclase generates the second messenger cyclic AMP |
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266 | (1) |
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Cyclic AMP activates protein kinase A |
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267 | (1) |
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Signaling pathways are also switched off |
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267 | (2) |
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The phosphoinositide signaling pathway generates two second messengers |
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269 | (1) |
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Calmodulin mediates some Ca2+ signals |
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270 | (1) |
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10.3 Receptor Tyrosine Kinases |
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270 | (3) |
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The insulin receptor dimer binds one insulin |
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271 | (1) |
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The receptor undergoes autophosphorylation |
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271 | (2) |
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Box 10.13 Cell Signaling and Cancer |
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273 | (1) |
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10.4 Lipid Hormone Signaling |
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274 | (2) |
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Eicosanoids are short-range signals |
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275 | (1) |
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Box 10.0 Aspirin and Other Inhibitors of Cyclooxygenase |
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276 | (7) |
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283 | (18) |
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283 | (4) |
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Most carbohydrates are chiral compounds |
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284 | (1) |
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Cyclization generates a and p anomers |
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285 | (1) |
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Monosaccharides can be derivatized in many different ways |
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286 | (1) |
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287 | (3) |
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Lactose and sucrose are the most common disaccharides |
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288 | (1) |
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Starch and glycogen are fuel-storage molecules |
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288 | (1) |
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Cellulose and chitin provide structural support |
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289 | (1) |
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Box 11.A Cellulosic Biofuel |
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290 | (1) |
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Bacterial polysaccharides form a biofilm |
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291 | (1) |
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291 | (2) |
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Oligosaccharides are N-linked or O-linked |
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292 | (1) |
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Oligosaccharide groups are biological markers |
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293 | (1) |
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Box 11.B The ABO Blood Group System |
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293 | (8) |
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Proteoglycans contain long glycosaminoglycan chains |
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294 | (1) |
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Bacterial cell walls are made of peptidoglycan |
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295 | (6) |
| Part 3 Metabolism |
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12 Metabolism and Bioenergetics |
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301 | (28) |
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301 | (2) |
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Cells take up the products of digestion |
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302 | (1) |
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Box 12.A Dietary Guidelines |
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303 | (3) |
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Monomers are stored as polymers |
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304 | (1) |
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Fuels are mobilized as needed |
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304 | (2) |
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306 | (5) |
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Some major metabolic pathways share a few common intermediates |
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307 | (1) |
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Many metabolic pathways include oxidation-reduction reactions |
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308 | (2) |
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Metabolic pathways are complex |
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310 | (1) |
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Box 12.B The Transcriptome, the Proteome, and the Metabolome |
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311 | (3) |
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Human metabolism depends on vitamins |
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312 | (2) |
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12.3 Free Energy Changes in Metabolic Reactions |
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314 | (6) |
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The free energy change depends on reactant concentrations |
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314 | (2) |
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Unfavorable reactions are coupled to favorable reactions |
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316 | (2) |
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Free energy can take different forms |
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318 | (2) |
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Box 12.0 Powering Human Muscles |
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320 | (9) |
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Regulation occurs at the steps with the largest free energy changes |
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321 | (8) |
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329 | (33) |
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330 | (10) |
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Reactions 1-5 are the energy-investment phase of glycolysis |
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330 | (6) |
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Reactions 6-10 are the energy-payoff phase of glycolysis |
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336 | (4) |
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Box 13.A Catabolism of Other Sugars |
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340 | (2) |
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Pyruvate is converted to other substances |
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341 | (1) |
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Box 13.B Alcohol Metabolism |
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342 | (2) |
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344 | (3) |
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Four gluconeogenic enzymes plus some glycolytic enzymes convert pyruvate to glucose |
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345 | (1) |
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Gluconeogenesis is regulated at the fructose bisphosphatase step |
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346 | (1) |
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13.3 Glycogen Synthesis and Degradation |
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347 | (3) |
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Glycogen synthesis consumes the free energy of UTP |
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348 | (1) |
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Glycogen phosphorylase catalyzes glycogenolysis |
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349 | (1) |
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13.4 The Pentose Phosphate Pathway |
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350 | (3) |
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The oxidative reactions of the pentose phosphate pathway produce NADPH |
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350 | (1) |
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Isomerization and interconversion reactions generate a variety of monosaccharides |
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351 | (1) |
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A summary of glucose metabolism |
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352 | (1) |
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13.5 Clinical Connection: Disorders of Carbohydrate Metabolism |
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353 | (9) |
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Glycogen storage diseases affect liver and muscle |
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354 | (8) |
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362 | (23) |
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14.1 The Pyruvate Dehydrogenase Reaction |
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362 | (3) |
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The pyruvate dehydrogenase complex contains multiple copies of three different enzymes |
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363 | (1) |
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Pyruvate dehydrogenase converts pyruvate to acetyl-CoA |
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363 | (2) |
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14.2 The Eight Reactions of the Citric Acid Cycle |
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365 | (7) |
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1 Citrate synthase adds an acetyl group to oxaloacetate |
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366 | (2) |
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2 Aconitase isomerizes citrate to isocitrate |
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368 | (1) |
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3 Isocitrate dehydrogenase releases the first CO2 |
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369 | (1) |
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4 α-Ketoglutarate dehydrogenase releases the second CO2 |
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369 | (1) |
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5 Succinyl-CoA synthetase catalyzes substrate-level phosphorylation |
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370 | (1) |
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6 Succinate dehydrogenase generates ubiquinol |
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370 | (1) |
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7 Fumarase catalyzes a hydration reaction |
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371 | (1) |
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8 Malate dehydrogenase regenerates oxaloacetate |
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371 | (1) |
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14.3 Thermodynamics of the Citric Acid Cycle |
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372 | (1) |
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The citric acid cycle is an energy-generating catalytic cycle |
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372 | (1) |
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The citric acid cycle is regulated at three steps |
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372 | (1) |
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The citric acid cycle probably evolved as a synthetic pathway |
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373 | (1) |
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Box 14.A Mutations in Citric Acid Cycle Enzymes |
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373 | (2) |
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14.4 Anabolic and Catabolic Functions of the Citric Acid Cycle |
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375 | (2) |
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Citric acid cycle intermediates are precursors of other molecules |
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375 | (1) |
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Anaplerotic reactions replenish citric acid cycle intermediates |
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376 | (1) |
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Box 14.B The Glyoxylate Pathway |
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377 | (8) |
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15 Oxidative Phosphorylation |
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385 | (26) |
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15.1 The Thermodynamics of Oxidation-Reduction Reactions |
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385 | (5) |
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Reduction potential indicates a substance's tendency to accept electrons |
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386 | (2) |
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The free energy change can be calculated from the change in reduction potential |
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388 | (2) |
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15.2 Mitochondrial Electron Transport |
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390 | (8) |
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Mitochondrial membranes define two compartments |
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390 | (2) |
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Complex I transfers electrons from NADH to ubiquinone |
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392 | (2) |
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Other oxidation reactions contribute to the ubiquinol pool |
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394 | (1) |
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Complex III transfers electrons from ubiquinol to cytochrome c |
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394 | (3) |
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Complex IV oxidizes cytochrome c and reduces O2 |
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397 | (1) |
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Box 15.A Free Radicals and Aging |
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398 | (1) |
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399 | (2) |
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Chemiosmosis links electron transport and oxidative phosphorylation |
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400 | (1) |
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The proton gradient is an electrochemical gradient |
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400 | (1) |
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401 | (3) |
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ATP synthase rotates as it translocates protons |
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401 | (2) |
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The binding change mechanism explains how ATP is made |
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403 | (1) |
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The P:O ratio describes the stoichiometry of oxidative phosphorylation |
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403 | (1) |
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Box 15.B Uncoupling Agents Prevent ATP Synthesis |
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404 | (7) |
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The rate of oxidative phosphorylation depends on the rate of fuel catabolism |
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404 | (7) |
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411 | (21) |
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16.1 Chloroplasts and Solar Energy |
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411 | (4) |
|
Pigments absorb light of different wavelengths |
|
|
412 | (2) |
|
Light-harvesting complexes transfer energy to the reaction center |
|
|
414 | (1) |
|
|
|
415 | (7) |
|
Photosystem II is a light-activated oxidation-reduction enzyme |
|
|
416 | (1) |
|
The oxygen-evolving complex of Photosystem II oxidizes water |
|
|
417 | (1) |
|
Cytochrome b6f links Photosystems I and II |
|
|
418 | (1) |
|
A second photooxidation occurs at Photosystem I |
|
|
419 | (2) |
|
Chemiosmosis provides the free energy for ATP synthesis |
|
|
421 | (1) |
|
|
|
422 | (2) |
|
Rubisco catalyzes CO2 fixation |
|
|
422 | (2) |
|
|
|
424 | (8) |
|
The Calvin cycle rearranges sugar molecules |
|
|
424 | (2) |
|
The availability of light regulates carbon fixation |
|
|
426 | (1) |
|
Calvin cycle products are used to synthesize sucrose and starch |
|
|
426 | (6) |
|
|
|
432 | (32) |
|
|
|
432 | (3) |
|
17.2 Fatty Acid Oxidation |
|
|
435 | (8) |
|
Fatty acids are activated before they are degraded |
|
|
435 | (1) |
|
Each round of β oxidation has four reactions |
|
|
436 | (3) |
|
Degradation of unsaturated fatty acids requires isomerization and reduction |
|
|
439 | (1) |
|
Oxidation of odd-chain fatty acids yields propionyl-CoA |
|
|
440 | (2) |
|
Some fatty acid oxidation occurs in peroxisomes |
|
|
442 | (1) |
|
17.3 Fatty Acid Synthesis |
|
|
443 | (5) |
|
Acetyl-CoA carboxylase catalyzes the first step of fatty acid synthesis |
|
|
444 | (1) |
|
Fatty acid synthase catalyzes seven reactions |
|
|
445 | (2) |
|
Other enzymes elongate and desaturate newly synthesized fatty acids |
|
|
447 | (1) |
|
Box 17.A Fats, Diet, and Heart Disease |
|
|
448 | (2) |
|
Fatty acid synthesis can be activated and inhibited |
|
|
449 | (1) |
|
Box 17.B Inhibitors of Fatty Acid Synthesis |
|
|
450 | (2) |
|
Acetyl-CoA can be converted to ketone bodies |
|
|
450 | (2) |
|
17.4 Synthesis of Other Lipids |
|
|
452 | (12) |
|
Triacylglycerols and phospholipids are built from acyl-CoA groups |
|
|
452 | (2) |
|
Cholesterol synthesis begins with acetyl-CoA |
|
|
454 | (3) |
|
A summary of lipid metabolism |
|
|
457 | (7) |
|
|
|
464 | (33) |
|
18.1 Nitrogen Fixation and Assimilation |
|
|
464 | (5) |
|
Nitrogenase converts N2 to NH3 |
|
|
465 | (1) |
|
Ammonia is assimilated by glutamine synthetase and glutamate synthase |
|
|
466 | (1) |
|
Transamination moves amino groups between compounds |
|
|
467 | (2) |
|
Box 18.A Transaminases in the Clinic |
|
|
469 | (1) |
|
18.2 Amino Acid Biosynthesis |
|
|
469 | (4) |
|
Several amino acids are easily synthesized from common metabolites |
|
|
470 | (1) |
|
Amino acids with sulfur, branched chains, or aromatic groups are more difficult to synthesize |
|
|
471 | (2) |
|
Box 18.B Glyphosate, the Most Popular Herbicide |
|
|
473 | (3) |
|
Amino acids are the precursors of some signaling molecules |
|
|
475 | (1) |
|
|
|
476 | (1) |
|
18.3 Amino Acid Catabolism |
|
|
476 | (4) |
|
Amino acids are glucogenic, ketogenic, or both |
|
|
477 | (3) |
|
Box 18.D Diseases of Amino Acid Metabolism |
|
|
480 | (1) |
|
18.4 Nitrogen Disposal: The Urea Cycle |
|
|
480 | (5) |
|
Glutamate supplies nitrogen to the urea cycle |
|
|
481 | (1) |
|
The urea cycle consists of four reactions |
|
|
482 | (3) |
|
18.5 Nucleotide Metabolism |
|
|
485 | (12) |
|
Purine nucleotide synthesis yields IMP and then AMP and GMP |
|
|
485 | (1) |
|
Pyrimidine nucleotide synthesis yields UTP and CTP |
|
|
486 | (1) |
|
Ribonucleotide reductase converts ribonucleotides to deoxyribonucleotides |
|
|
487 | (1) |
|
Thymidine nucleotides are produced by methylation |
|
|
488 | (1) |
|
Nucleotide degradation produces uric acid or amino acids |
|
|
489 | (8) |
|
19 Regulation of Mammalian Fuel Metabolism |
|
|
497 | (22) |
|
19.1 Integration of Fuel Metabolism |
|
|
498 | (2) |
|
Organs are specialized for different functions |
|
|
498 | (1) |
|
Metabolites travel between organs |
|
|
499 | (1) |
|
Box 19.A The Intestinal Microbiome Contributes to Metabolism |
|
|
500 | (1) |
|
19.2 Hormonal Control of Fuel Metabolism |
|
|
501 | (6) |
|
Insulin is released in response to glucose |
|
|
502 | (1) |
|
Insulin promotes fuel use and storage |
|
|
503 | (1) |
|
Glucagon and epinephrine trigger fuel mobilization |
|
|
504 | (1) |
|
Additional hormones influence fuel metabolism |
|
|
505 | (1) |
|
AMP-dependent protein kinase acts as a fuel sensor |
|
|
506 | (1) |
|
19.3 Disorders of Fuel Metabolism |
|
|
507 | (1) |
|
The body generates glucose and ketone bodies during starvation |
|
|
507 | (1) |
|
Box 19.B Marasmus and Kwashiorkor |
|
|
507 | (4) |
|
Obesity has multiple causes |
|
|
508 | (1) |
|
Diabetes is characterized by hyperglycemia |
|
|
509 | (2) |
|
The metabolic syndrome links obesity and diabetes |
|
|
511 | (1) |
|
19.4 Clinical Connection: Cancer Metabolism |
|
|
511 | (8) |
|
Aerobic glycolysis supports biosynthesis |
|
|
512 | (1) |
|
Cancer cells consume large amounts of glutamine |
|
|
512 | (7) |
| Part 4 Genetic Information |
|
|
20 DNA Replication and Repair |
|
|
519 | (32) |
|
20.1 The DNA Replication Machinery |
|
|
519 | (9) |
|
Replication occurs in factories |
|
|
520 | (1) |
|
Helicases convert double-stranded DNA to single-stranded DNA |
|
|
521 | (1) |
|
DNA polymerase faces two problems |
|
|
522 | (1) |
|
DNA polymerases share a common structure and mechanism |
|
|
523 | (2) |
|
DNA polymerase proofreads newly synthesized DNA |
|
|
525 | (1) |
|
An RNase and a ligase are required to complete the lagging strand |
|
|
525 | (3) |
|
|
|
528 | (2) |
|
Telomerase extends chromosomes |
|
|
529 | (1) |
|
Box 20.A HIV Reverse Transcriptase |
|
|
530 | (1) |
|
Is telomerase activity linked to cell immortality? |
|
|
531 | (1) |
|
20.3 DNA Damage and Repair |
|
|
531 | (7) |
|
DNA damage is unavoidable |
|
|
531 | (2) |
|
Repair enzymes restore some types of damaged DNA |
|
|
533 | (1) |
|
Base excision repair corrects the most frequent DNA lesions |
|
|
533 | (2) |
|
Nucleotide excision repair targets the second most common form of DNA damage |
|
|
535 | (1) |
|
Double-strand breaks can be repaired by joining the ends |
|
|
535 | (1) |
|
Recombination also restores broken DNA molecules |
|
|
536 | (2) |
|
20.4 Clinical Connection: Cancer as a Genetic Disease |
|
|
538 | (2) |
|
Tumor growth depends on multiple events |
|
|
538 | (1) |
|
DNA repair pathways are closely linked to cancer |
|
|
539 | (1) |
|
|
|
540 | (11) |
|
DNA is negatively supercoiled |
|
|
541 | (1) |
|
Topoisomerases alter DNA supercoiling |
|
|
541 | (2) |
|
Eukaryotic DNA is packaged in nucleosomes |
|
|
543 | (8) |
|
|
|
551 | (29) |
|
21.1 Initiating Transcription |
|
|
552 | (6) |
|
|
|
552 | (1) |
|
DNA packaging affects transcription |
|
|
553 | (2) |
|
DNA also undergoes covalent modification |
|
|
555 | (1) |
|
Transcription begins at promoters |
|
|
555 | (2) |
|
Transcription factors recognize eukaryotic promoters |
|
|
557 | (1) |
|
Enhancers and silencers act at a distance from the promoter |
|
|
558 | (1) |
|
Box 21.A DNA-Binding Proteins |
|
|
558 | (4) |
|
Prokaryotic operons allow coordinated gene expression |
|
|
560 | (2) |
|
|
|
562 | (5) |
|
RNA polymerases have a common structure and mechanism |
|
|
562 | (2) |
|
RNA polymerase is a processive enzyme |
|
|
564 | (1) |
|
Transcription elongation requires a conformational change in RNA polymerase |
|
|
564 | (1) |
|
Transcription is terminated in several ways |
|
|
565 | (2) |
|
|
|
567 | (13) |
|
Eukaryotic mRNAs receive a 5' cap and a 3' poly(A) tail |
|
|
567 | (1) |
|
Splicing removes introns from eukaryotic RNA |
|
|
567 | (2) |
|
mRNA turnover and RNA interference limit gene expression |
|
|
569 | (3) |
|
rRNA and tRNA processing includes the addition, deletion, and modification of nucleotides |
|
|
572 | (1) |
|
RNAs have extensive secondary structure |
|
|
573 | (7) |
|
|
|
580 | |
|
22.1 tRNA and the Genetic Code |
|
|
580 | (5) |
|
The genetic code is redundant |
|
|
581 | (1) |
|
tRNAs have a common structure |
|
|
581 | (1) |
|
tRNA aminoacylation consumes ATP |
|
|
582 | (2) |
|
Some synthetases have proofreading activity |
|
|
584 | (1) |
|
tRNA anticodons pair with mRNA codons |
|
|
584 | (1) |
|
Box 22.A The Genetic Code Expanded |
|
|
585 | (1) |
|
|
|
586 | (3) |
|
The ribosome is mostly RNA |
|
|
586 | (1) |
|
Three tRNAs bind to the ribosome |
|
|
587 | (2) |
|
|
|
589 | (5) |
|
Initiation requires an initiator tRNA |
|
|
589 | (1) |
|
The appropriate tRNAs are delivered to the ribosome during elongation |
|
|
590 | (3) |
|
The peptidyl transferase active site catalyzes peptide bond formation |
|
|
593 | (1) |
|
Box 22.B Antibiotic Inhibitors of Protein Synthesis |
|
|
594 | (3) |
|
Release factors mediate translation termination |
|
|
595 | (1) |
|
Translation is efficient in vivo |
|
|
596 | (1) |
|
22.4 Post-Translational Events |
|
|
597 | |
|
Chaperones promote protein folding |
|
|
597 | (2) |
|
The signal recognition particle targets some proteins for membrane translocation |
|
|
599 | (1) |
|
Many proteins undergo covalent modification |
|
|
600 | |
| Glossary |
|
G-1 | |
| Odd-Numbered Solutions |
|
S-1 | |
| Index |
|
1-1 | |
