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Figure 1-1 Four examples of biochemical functions performed by proteins
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Figure 1-2 Levels of protein structure illustrated by the catabolite activator protein
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Figure 1-3 Amino-acid structure and the chemical characters of the amino-acid side chains
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Figure 1-4 The genetic code
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Figure 1-5 The flow of genetic information in prokaryotes (left) and eukaryotes (right)
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Figure 1-6 Table of the frequency with which one amino-acid is replaced by others in amino-acid sequences of the same protein from different organisms
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Figure 1-7 Peptide bond formation and hydrolysis
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Figure 1-8 Schematic diagram of an extended polypeptide chain
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Figure 1-9 Extended polypeptide chain showing the typical backbone bond lengths and angles
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Figure 1-10 Table of the typical chemical interactions that stabilize polypeptides
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Figure 1-11 Ramachandran plot
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Figure 1-12 Typical beta turn
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Figure 1-13 The alpha helix
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Figure 1-14 Table of helical parameters
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Figure 1-15 View along the axis of an idealized alpha-helical polypeptide
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Figure 1-16 The structure of collagen
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Figure 1-17 The structure of the beta sheet
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Figure 1-18 Two proteins that form a complex through hydrogen bonding between beta strands (the rap–raf complex, PDB 1gua)
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Figure 1-19 Beta barrel
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Figure 1-20 Table of conformational preferences of the amino acids
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Figure 1-21 An example of secondary structure prediction
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Figure 1-22 Folding intermediates
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Figure 1-23 Highly simplified schematic representation of the folding of a polypeptide chain in water
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Figure 1-24 Comparison of the structures of triosephosphate isomerase and dihydrofolate reductase
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Figure 1-25 Variable loops
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Figure 1-26 Porcine pancreatic elastase showing the first hydration shell surrounding the protein
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Figure 1-27 Cut-away view of the interior of a folded protein
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Figure 1-28 Packing motifs of a helical structure
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Figure 1-29 A segment of a simulated membrane bilayer
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Figure 1-30 The three-dimensional structure of part of the cytochrome bc1 complex
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Figure 1-31 Hydropathy plot of the Rhizobium meliloti protein DctB
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Figure 1-32 The three-dimensional structure of the all-beta transport protein FhuA
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Figure 1-33 Three-dimensional structure of the bacterial potassium channel
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Figure 1-34 Illustration of the ordered arrays of water molecules surrounding exposed hydrophobic residues in bovine pancreatic ribonuclease A
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Figure 1-35 Computed circular dichroism spectra for the evaluation of protein conformation
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Figure 1-36 Results of a molecular dynamics simulation of two interacting alpha helices
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Figure 1-37 The structure of the small protein bovine pancreatic trypsin inhibitor, BPTI
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Figure 1-38 Stabilization by coordinate covalent bonds
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Figure 1-39 Examples of stabilization by cofactor binding
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Figure 1-40 Table of post-translational modifications affecting protein stability
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Figure 1-41 Schematic diagram of the Lac repressor tetramer binding to DNA
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Figure 1-42 Structure of alanine racemase
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Figure 1-43 Structures of thioesterase and thioester dehydrase
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Figure 1-44 Structure of gamma-crystallin
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Figure 1-45 Structures of tryptophan synthase and galactonate dehydratase
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Figure 1-46 Schematic diagram of the domain arrangement of a number of signal transduction proteins
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Figure 1-47 Structures of aldose reductase (left) and phosphotriesterase (right)
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Figure 1-48 Structures of aspartate aminotransferase (top) and D-amino acid aminotransferase (bottom)
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Figure 1-49 Zinc finger motif
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Figure 1-50 Helix-turn-helix
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Figure 1-51 Four-helix bundle motif
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Figure 1-52 Catalytic triad
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Figure 1-53 TIM-barrel proteins
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Figure 1-54 Myohemerythrin
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Figure 1-55 Myoglobin
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Figure 1-56 Immunoglobulin
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Figure 1-57 Neuraminidase beta-propeller domain
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Figure 1-58 Pre-albumin
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Figure 1-59 Bacteriochlorophyll A protein
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Figure 1-60 Crossover connection between parallel beta strands
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Figure 1-61 Alpha/beta domains
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Figure 1-62 Alpha+beta saddle
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Figure 1-63 Disulfide-linked protein
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Figure 1-64 Zinc finger
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Figure 1-65 Schematic representations of different kinds of oligomers
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Figure 1-66 "Open-book" view of the complementary structural surfaces that form the interface between interleukin-4 (left) and its receptor (right)
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Figure 1-67 Coiled-coil alpha-helical interactions
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Figure 1-68 Peptide–peptide interactions in the coiled coil of the leucine zipper family of DNA-binding proteins
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Figure 1-69 Water molecules at a subunit interface
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Figure 1-70 Oligomerization by beta sheet formation
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Figure 1-71 Sickle-cell hemoglobin
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Figure 1-72 Dominant-negative phenotype resulting from hydrophobic interactions between mutant and normal subunits of a dimeric protein
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Figure 1-73 The human growth hormone–receptor complex
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Figure 1-74 Examples of quaternary arrangements observed for oligomeric proteins
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Figure 1-75 Interactions underlying different geometric arrangements of subunits
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Figure 1-76 Table of protein motions
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Figure 1-77 Triosephosphate isomerase
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Figure 1-78 Protein shaded according to flexibility
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Figure 1-79 T4 lysozyme
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Figure 1-80 Aspartate aminotransferase, open and closed forms
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