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Bio Ch 5 Pwpt
1. Chapter 5 The Structure and Function of Large Biological Molecules
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5. Fig. 5-2a Dehydration removes a water molecule, forming a new bond Short polymer Unlinked monomer Longer polymer Dehydration reaction in the synthesis of a polymer HO HO HO H 2 O H H H 4 3 2 1 1 2 3 (a)
6. Fig. 5-2b Hydrolysis adds a water molecule, breaking a bond Hydrolysis of a polymer HO HO HO H 2 O H H H 3 2 1 1 2 3 4 (b)
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10. Fig. 5-3 Dihydroxyacetone Ribulose Ketoses Aldoses Fructose Glyceraldehyde Ribose Glucose Galactose Hexoses (C 6 H 12 O 6 ) Pentoses (C 5 H 10 O 5 ) Trioses (C 3 H 6 O 3 )
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12. Fig. 5-4 (a) Linear and ring forms (b) Abbreviated ring structure
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14. Fig. 5-5 (b) Dehydration reaction in the synthesis of sucrose Glucose Fructose Sucrose Maltose Glucose Glucose (a) Dehydration reaction in the synthesis of maltose 1–4 glycosidic linkage 1–2 glycosidic linkage
20. Fig. 5-7 (a) and glucose ring structures Glucose Glucose (b) Starch: 1–4 linkage of glucose monomers (b) Cellulose: 1–4 linkage of glucose monomers
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25. Fig. 5-10 The structure of the chitin monomer. (a) (b) (c) Chitin forms the exoskeleton of arthropods. Chitin is used to make a strong and flexible surgical thread.
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28. Fig. 5-11 Fatty acid (palmitic acid) Glycerol (a) Dehydration reaction in the synthesis of a fat Ester linkage (b) Fat molecule (triacylglycerol)
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31. Fig. 5-12 Structural formula of a saturated fat molecule Stearic acid, a saturated fatty acid (a) Saturated fat Structural formula of an unsaturated fat molecule Oleic acid, an unsaturated fatty acid (b) Unsaturated fat cis double bond causes bending
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36. Fig. 5-13 (b) Space-filling model (a) (c) Structural formula Phospholipid symbol Fatty acids Hydrophilic head Hydrophobic tails Choline Phosphate Glycerol Hydrophobic tails Hydrophilic head
48. Fig. 5-17a Nonpolar Glycine (Gly or G) Alanine (Ala or A) Valine (Val or V) Leucine (Leu or L) Isoleucine (Ile or ) Methionine (Met or M) Phenylalanine (Phe or F) Tryptophan (Trp or W) Proline (Pro or P)
49. Fig. 5-17b Polar Asparagine (Asn or N) Glutamine (Gln or Q) Serine (Ser or S) Threonine (Thr or T) Cysteine (Cys or C) Tyrosine (Tyr or Y)
50. Fig. 5-17c Acidic Arginine (Arg or R) Histidine (His or H) Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Basic Electrically charged
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52. Peptide bond Fig. 5-18 Amino end (N-terminus) Peptide bond Side chains Backbone Carboxyl end (C-terminus) (a) (b)
63. Fig. 5-22 Primary structure Secondary and tertiary structures Quaternary structure Normal hemoglobin (top view) Primary structure Secondary and tertiary structures Quaternary structure Function Function subunit Molecules do not associate with one another; each carries oxygen. Red blood cell shape Normal red blood cells are full of individual hemoglobin moledules, each carrying oxygen. 10 µm Normal hemoglobin 1 2 3 4 5 6 7 Val His Leu Thr Pro Glu Glu Red blood cell shape subunit Exposed hydrophobic region Sickle-cell hemoglobin Molecules interact with one another and crystallize into a fiber; capacity to carry oxygen is greatly reduced. Fibers of abnormal hemoglobin deform red blood cell into sickle shape. 10 µm Sickle-cell hemoglobin Glu Pro Thr Leu His Val Val 1 2 3 4 5 6 7
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65. Fig. 5-23 Normal protein Denatured protein Denaturation Renaturation
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67. Fig. 5-24 Hollow cylinder Cap Chaperonin (fully assembled) Polypeptide Steps of Chaperonin Action: An unfolded poly- peptide enters the cylinder from one end. 1 2 3 The cap attaches, causing the cylinder to change shape in such a way that it creates a hydrophilic environment for the folding of the polypeptide. The cap comes off, and the properly folded protein is released. Correctly folded protein
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70. Fig. 5-26-3 mRNA Synthesis of mRNA in the nucleus DNA NUCLEUS mRNA CYTOPLASM Movement of mRNA into cytoplasm via nuclear pore Ribosome Amino acids Polypeptide Synthesis of protein 1 2 3
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73. Fig. 5-27c-2 Ribose (in RNA) Deoxyribose (in DNA) Sugars (c) Nucleoside components: sugars
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75. Fig. 5-27 5’ end Nucleoside Nitrogenous base Phosphate group Sugar (pentose) (b) Nucleotide (a) Polynucleotide, or nucleic acid 3’ end 3 C 3 C 5 C 5 C Nitrogenous bases Pyrimidines Cytosine (C) Thymine (T, in DNA) Uracil (U, in RNA) Purines Adenine (A) Guanine (G) Sugars Deoxyribose (in DNA) Ribose (in RNA) (c) Nucleoside components: sugars
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77. Fig. 5-28 Sugar-phosphate backbones 3' end 3' end 3' end 3' end 5' end 5' end 5' end 5' end Base pair (joined by hydrogen bonding) Old strands New strands Nucleotide about to be added to a new strand
Figure 5.2 The synthesis and breakdown of polymers
Figure 5.2 The synthesis and breakdown of polymers
Figure 5.3 The structure and classification of some monosaccharides
Figure 5.4 Linear and ring forms of glucose
Figure 5.5 Examples of disaccharide synthesis
Figure 5.6 Storage polysaccharides of plants and animals
Figure 5.7 Starch and cellulose structures
Figure 5.8 The arrangement of cellulose in plant cell walls
Figure 5.10 Chitin, a structural polysaccharide
Figure 5.11 The synthesis and structure of a fat, or triacylglycerol
Figure 5.12 Examples of saturated and unsaturated fats and fatty acids
Figure 5.13 The structure of a phospholipid
Figure 5.14 Bilayer structure formed by self-assembly of phospholipids in an aqueous environment
For the Cell Biology Video Space Filling Model of Cholesterol, go to Animation and Video Files. For the Cell Biology Video Stick Model of Cholesterol, go to Animation and Video Files.
Figure 5.15 Cholesterol, a steroid
Table 5-1
Figure 5.16 The catalytic cycle of an enzyme
Figure 5.17 The 20 amino acids of proteins
Figure 5.17 The 20 amino acids of proteins
Figure 5.17 The 20 amino acids of proteins
Figure 5.18 Making a polypeptide chain
For the Cell Biology Video An Idealized Alpha Helix: No Sidechains, go to Animation and Video Files. For the Cell Biology Video An Idealized Alpha Helix, go to Animation and Video Files. For the Cell Biology Video An Idealized Beta Pleated Sheet Cartoon, go to Animation and Video Files. For the Cell Biology Video An Idealized Beta Pleated Sheet, go to Animation and Video Files.
Figure 5.21 Levels of protein structure — secondary structure
Figure 5.21 Levels of protein structure — tertiary and quaternary structures
Figure 5.21 Levels of protein structure — tertiary and quaternary structures
Figure 5.22 A single amino acid substitution in a protein causes sickle-cell disease
Figure 5.23 Denaturation and renaturation of a protein
Figure 5.24 A chaperonin in action
Figure 5.26 DNA -> RNA -> protein
Figure 5.27 Components of nucleic acids
Figure 5.27 Components of nucleic acids
Figure 5.28 The DNA double helix and its replication
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