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Chemistry of Life Macromolecules Macromolecules • Smaller molecules linked together to create large molecules – Polymerization – Have specific 3d shape • Proteins - enzymes, hormones, structure, transport • Carbohydrates – storage, structure Macromolecules • Carbon’s properties enable it to make many different molecules Isomers = molecules with the same formula but different structural formulae Specific 3d shape Ethane Functional group Ethanol Functional groups Create the necessary variety of shapes of macromolecules for life to exist Dehydration synthesis = enzymatically controlled formation of macromolecules by removal of water Macromolecules • Macromolecules are broken down (catalyzed) by HYDROLYSIS (‘water splitting’) • Requires specific enzyme(s) Check Point • • • • • • What are macromolecules? Why is carbon so important to life? What are functional groups? How are macromolecules formed? How are macromolecules broken down? What molecule makes up most organisms? Macromolecules Important to Life • • • • Carbohydrates Lipids Proteins Nucleic acids Macromolecules • What do you need to know for each macromolecule: – Monomers – Function in organisms Carbohydrates: • Carbon + water (hydrate) • Monomers = monosaccharide • Monosaccharides – sugars – Glucose – Fructose – Galactose – Ribose – Deoxyribose Monosaccharides • Monomers may be functional: – Glucose is primary source of energy for organisms • Glucose - C6H12O6 • Many monomers form rings in solutions to become more stable Carbohydrates • • • • • Monosaccharide + monosaccharide = Disaccharide Glucose + glucose = maltose Glucose + fructose = sucrose Glucose + galactose = lactose Polysaccharides • Polymers of monosaccharides • Type of monosaccharide and arrangement creates variability in polysaccharides – Starch (Amylose, amylopectin) = plants – Glycogen = glucose storage for animals – Cellulose = plant cell walls – Chitin = exoskeleton of arthropods, some fungi Carbohydrates: Function • Energy; stored energy _____(?) • Structure – ___________(?) • Cell-to-cell communication, identification (glycoproteins, glycolipids) ______(?) Lipids • Insoluble in water; (long, nonpolar hydrocarbon chains) • Three types: – Fats, oils, waxes – Phospholipids – Steroids Lipids: Fats • Macromolecules of glycerol + 3 fatty acids • Fatty acids = hydrocarbon chain (16-18 carbons) • Fats = triglycerides (3 fatty acids) • Structure of the fatty acid chains creates different kinds of fats Fats • Fatty acids may have more or less carbons atoms in their chains • Carbon atoms may be double bonded – Double bonds reduce the number of hydrogen atoms in the chain – Causes chain to bend Fats • Fatty acid chains with double bonds have less hydrogen • Chains with the maximum amount of hydrogen (no double bonds) are said to be ‘saturated’ • Chains with less than the maximum are said to be ‘unsaturated’ Types of Fats • • • • • Saturated No double bonds Solids @ (200) Animal fats Bacon grease, lard, butter • • • • • Unsaturated Double bond(s) Liquids @ (200) Plant fats (oil) Corn, peanut, olive oils Triglycerides • • • • • Important to diet Limit amount of saturated fats Hydrocarbon chains are high in energy More difficult to breakdown Link to triglycerides and arteriosclerosis Lipids: Phospholipids • Glycerol + 2 fatty acids • 3rd position on the glycerol is taken by a phosphate group • Major component of cell membrane Lipids: Steroids • 4 fused carbon rings • Cholesterol – Cell membranes – Help to moderate the effects of extreme temperatures • Precursors of sex hormones – estrogen, testosterone • Too much causes atherosclerosis (?) Cholesterol Proteins • • • • • Many shapes = many functions Polymers of AMINO ACIDS Linked by PEPTIDE BONDS POLYPEPTIDES Proteins = folded, shaped polypeptides Proteins: Amino Acids • 20 different amino acids • R group determines properties of the amino acid • May be nonpolar, or polar; acidic or alkaline • Essential amino acids - body cannot produce on its own, must be part of the diet Tremendous Variety Proteins • Peptide bonds are produced by DEHYDRATION SYNTHESIS • String of polypeptide bonds - POLYPEPTIDE Proteins • • • • Function depends upon shape Globular Fibrous = ‘stringy’ CONFORMATION = 3d shape caused by Hbonds – Fold and twist the amino acids Protein Structure • Sequence of amino acids – Determined by genetic code – ‘Goof’ in sequence can have harmful or lethal effects Denaturation • Alteration of conformational shape • Caused by: – Heat – body T – pH – Salinity – Organic solvents (alcohols, acetone, etc.) – Inorganic chemicals that dissolve bonds (HCl) Denaturation • Some proteins change shape in order to function – Receptor, contractile Nucleic Acids • DNA, RNA • Polymers of nucleotides • Nucleotide: – Simple sugar (ribose or deoxyribose) – Nitrogenous base – Phosphate group (PO4) 4 nitrogenous bases; Nucleic Acids • • • • • Nitrogenous bases are complimentary A-T C-G Hydrogen bonds Sugar-phosphate backbone H bonding Relationship between nucleic acids and proteins