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Unit 1 – The Chemistry of LifeUnit 1 – The Chemistry of Life
Chapter 5 ~
The Structure & Function of Macromolecules
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PolymersPolymers
• Covalent monomers• Condensation reaction
(dehydration reaction):One monomer
provides a hydroxyl group while the other provides a hydrogen to form a water molecule
• Hydrolysis:bonds between
monomers are broken by adding water (digestion)
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Carbohydrates, ICarbohydrates, I
• Monosaccharides √ CH2O formula; √ multiple hydroxyl (-OH) groups and 1 carbonyl (C=O) group: aldehyde (aldoses) sugar ketone sugar √ cellular respiration; √ raw material for amino acids and fatty acids
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Carbohydrates, IICarbohydrates, II
• Disaccharides √ glycosidic linkage (covalent
bond) between 2 monosaccharides;
√ covalent bond by dehydration reaction
• Sucrose (table sugar) √ most common disaccharide
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Carbohydrates, IIICarbohydrates, III
• Polysaccharides Storage: Starch~ glucose monomers Plants: plastids Animals: glycogen
• Polysaccharides Structural: Cellulose~ most abundant
organic compound; Chitin~ exoskeletons; cell walls of fungi; surgical thread
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LipidsLipids• No polymers; glycerol and fatty acid
• Fats, phospholipids, steroids
• Hydrophobic; H bonds in water exclude fats
• Carboxyl group = fatty acid
• Non-polar C-H bonds in fatty acid ‘tails’
• Ester linkage: 3 fatty acids to 1 glycerol (dehydration formation)
• Triacyglycerol (triglyceride)
• Saturated vs. unsaturated fats; single vs. double
• bonds
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PhospholipidsPhospholipids
• 2 fatty acids instead of 3 (phosphate group)
• ‘Tails’ hydrophobic; ‘heads’ hydrophilic
• Micelle (phospholipid droplet in water)
• Bilayer (double layer);cell membranes
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SteroidsSteroids
• Lipids with 4 fused carbon rings
• Ex: cholesterol:cell membranes;precursor for other steroids (sex hormones); atherosclerosis
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ProteinsProteins
• Importance: instrumental in nearly everything organisms do; 50% dry weight of cells; most structurally sophisticated molecules known
• Monomer: amino acids (there are 20) ~ carboxyl (-COOH) group, amino group (NH2), H atom, variable group (R)….
• Variable group characteristics: polar (hydrophilic), nonpolar (hydrophobic), acid or base
• Three-dimensional shape (conformation)• Polypeptides (dehydration reaction): peptide
bonds~ covalent bond; carboxyl group to amino group (polar)
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Primary StructurePrimary Structure
• Conformation: Linear structure
• Molecular Biology: each type of protein has a unique primary structure of amino acids
• Ex: lysozyme
• Amino acid substitution:hemoglobin; sickle-cell anemia
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Secondary StructureSecondary Structure
• Conformation: coils & folds (hydrogen bonds)
• Alpha Helix: coiling; keratin
• Pleated Sheet: parallel; silk
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Tertiary StructureTertiary Structure
• Conformation: irregular contortions from R group bonding√hydrophobic √disulfide bridges√hydrogen bonds
√ionic bonds
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Quaternary StructureQuaternary Structure
• Conformation: 2 or more polypeptide chains aggregated into 1 macromolecule√collagen (connective
tissue)√hemoglobin
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Review of four levels of protein Review of four levels of protein structures.structures.
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Denaturation and renaturation of Denaturation and renaturation of a protein.a protein.
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Nucleic Acids, INucleic Acids, I
• Deoxyribonucleic acid (DNA)
• Ribonucleic acid (RNA)
• DNA->RNA->protein• Polymers of nucleotides
(polynucleotide):nitrogenous basepentose sugarphosphate group
• Nitrogenous bases:
pyrimidines~cytosine, thymine, uracil purines~adenine, guanine
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Nucleic Acids, IINucleic Acids, II
• Pentoses:√ribose (RNA)√deoxyribose (DNA)√nucleoside (base + sugar)
• Polynucleotide:√phosphodiester linkages (covalent); phosphate + sugar
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Nucleic Acids, IIINucleic Acids, III
• Inheritance based on DNA replication
• Double helix (Watson & Crick - 1953) H bonds~ between paired bases van der Waals~ between stacked bases
• A to T; C to G pairing
• Complementary