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1 | (18) |
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1.1 What are proteins, and what are they for? |
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2 | (1) |
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3 | (1) |
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1.3 The spontaneous folding of proteins |
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4 | (3) |
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Protein structures in three-dimensions |
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4 | (3) |
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1.4 Proteins and genomics |
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7 | (1) |
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7 | (3) |
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Protein mass spectrometry |
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8 | (1) |
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Two-dimensional gel electrophoresis |
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8 | (2) |
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1.6 Regulation of protein activity |
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10 | (2) |
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12 | (1) |
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12 | (1) |
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1.8 Protein dysfunction, and disease |
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13 | (2) |
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1.9 Databases and web sites containing information about proteins |
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15 | (4) |
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19 | (36) |
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2.1 Proteins are formed of polypeptide chains |
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20 | (1) |
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21 | (2) |
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2.3 Protein folding and denaturation |
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23 | (4) |
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What stabilizes native states of proteins? |
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23 | (2) |
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The native structures of proteins are determined by their sequences of amino acids |
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25 | (2) |
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2.4 Cofactors and post-translational modifications |
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27 | (1) |
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2.5 Protein structures and their analysis |
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28 | (12) |
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Secondary structures: α-helices and β-sheets appear in many proteins |
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29 | (2) |
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Conformational angles define protein conformations |
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31 | (1) |
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Primary, secondary, tertiary, and quaternary structures |
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31 | (2) |
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Supersecondary structures |
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33 | (1) |
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34 | (1) |
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35 | (2) |
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37 | (2) |
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Intrinsically-disordered proteins (IDP) |
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39 | (1) |
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40 | (1) |
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40 | (4) |
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44 | (11) |
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Diseases of protein aggregation |
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47 | (8) |
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3 Isolation and Structure determination of proteins |
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55 | (22) |
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56 | (5) |
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Ammonium sulphate precipitation |
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57 | (2) |
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Size-exclusion chromatography |
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59 | (1) |
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Ion-exchange chromatography |
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60 | (1) |
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60 | (1) |
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Specific expression of a target protein |
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60 | (1) |
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3.2 Experimental methods of protein structure determination |
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61 | (8) |
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61 | (4) |
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Protein structure determination by nuclear magnetic resonance (NMR) spectroscopy |
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65 | (1) |
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66 | (3) |
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3.3 Protein structure prediction |
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69 | (8) |
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Critical Assessment of Structure Prediction--CASP |
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69 | (1) |
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69 | (1) |
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A Priori Structure Prediction |
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70 | (7) |
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77 | (34) |
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78 | (3) |
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81 | (5) |
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How do enzymes speed up reactions? |
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82 | (1) |
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83 | (2) |
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Regulation of enzyme activity |
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85 | (1) |
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86 | (4) |
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88 | (2) |
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4.4 Membrane proteins and receptors |
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90 | (1) |
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91 | (8) |
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92 | (1) |
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Specificity of passage: the potassium channel |
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92 | (1) |
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Cross-membrane transport with or against a concentration gradient: the mitochondrial electron-transport chain and ATP synthase |
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92 | (2) |
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94 | (3) |
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Voltage-Gated Channels: Transmission of the nerve impulse |
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97 | (2) |
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4.6 Signal reception and transduction |
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99 | (2) |
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G-protein-coupled receptors |
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100 | (1) |
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4.7 Classification of protein function |
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101 | (10) |
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103 | (2) |
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The Gene Ontology™ Consortium |
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105 | (2) |
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Prediction of protein function |
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107 | (4) |
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111 | (1) |
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5.1 Evolution is exploration |
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112 | (2) |
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5.2 The importance of regulation |
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114 | (3) |
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5.3 How do we measure the evolutionary divergence of proteins? |
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117 | (3) |
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5.4 The relationship between divergence of sequence and structure |
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120 | (1) |
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Changes affecting local regions of the genome |
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121 | (1) |
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The effects of post-transcriptional events |
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122 | (1) |
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Domain reassembly in evolution |
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123 | (2) |
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5.5 Pathways and limits in the divergence of sequence, structure, and function |
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125 | (4) |
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Divergence of function in the enolase superfamily |
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127 | (2) |
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5.6 Protein evolution on the lab bench |
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129 | (10) |
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129 | (5) |
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Computational protein design |
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134 | (5) |
| Glossary |
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139 | (6) |
| Index |
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145 | |
