2. Chemistry of Life Macromolecules

3. Smaller molecules linked together to create large molecules –Polymerization –Have specific 3d shape Proteins - enzymes, hormones, structure, transport Carbohydrates – storage, structure

4. Macromolecules Carbon’s properties enable it to make many different molecules

5. Isomers = molecules with the same formula but different structural formulae

6. Specific 3d shape

8. Ethane Ethanol Functional group

9. Functional groups - Create the necessary variety of shapes of macromolecules for life to exist

10. Dehydration synthesis = enzymatically controlled formation of macromolecules by removal of water

11. Macromolecules Macromolecules are broken down (catalyzed) by HYDROLYSIS (‘water splitting’) Requires specific enzyme(s)

12. 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?

13. Macromolecules Important to Life Carbohydrates Lipids Proteins Nucleic acids

14. Macromolecules What do you need to know for each macromolecule: –Monomers –Function in organisms

15. Carbohydrates : Carbon + water (hydrate) Monomers = monosaccharide Monosaccharides – sugars –Glucose –Fructose –Galactose –Ribose –Deoxyribose

16. Monosaccharides Monomers may be functional: –Glucose is primary source of energy for organisms Glucose - C 6 H 12 O 6 Many monomers form rings in solutions to become more stable

17. Carbohydrates Monosaccharide + monosaccharide = Disaccharide Glucose + glucose = maltose Glucose + fructose = sucrose Glucose + galactose = lactose

18. 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

21. Carbohydrates: Function Energy; stored energy _____(?) Structure – ___________(?) Cell-to-cell communication, identification (glycoproteins, glycolipids) ______(?)

22. Lipids InsolubleInsoluble in water; (long, nonpolar hydrocarbon chains) Three types: –Fats, oils, waxes –Phospholipids –Steroids

23. 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

25. 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

26. 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’

27. Types of Fats Saturated No double bonds Solids @ (20 0 ) Animal fats Bacon grease, lard, butter Unsaturated Double bond(s) Liquids @ (20 0 ) Plant fats (oil) Corn, peanut, olive oils

28. Triglycerides Important to diet Limit amount of saturated fats Hydrocarbon chains are high in energy More difficult to breakdown Link to triglycerides and arteriosclerosis

29. Lipids: Phospholipids Glycerol + 2 fatty acids 3 rd position on the glycerol is taken by a phosphate group Major component of cell membrane

31. 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 (?)

32. Cholesterol

33. Proteins Many shapes = many functions Polymers of AMINO ACIDS Linked by PEPTIDE BONDS POLYPEPTIDES Proteins = folded, shaped polypeptides

34. 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

37. Tremendous Variety

38. Proteins Peptide bonds are produced by DEHYDRATION SYNTHESIS String of polypeptide bonds - POLYPEPTIDE

39. Proteins Function depends upon shape Globular Fibrous = ‘stringy’ CONFORMATION = 3d shape caused by H- bonds –Fold and twist the amino acids

43. Protein Structure Sequence of amino acids –Determined by genetic code –‘Goof’ in sequence can have harmful or lethal effects

44. Denaturation Alteration of conformational shape Caused by: –Heat – body T –pH - –Salinity –Organic solvents (alcohols, acetone, etc.) –Inorganic chemicals that dissolve bonds (HCl)

45. Denaturation Some proteins change shape in order to function –Receptor, contractile

47. Nucleic Acids DNA, RNA Polymers of nucleotides Nucleotide: –Simple sugar (ribose or deoxyribose) –Nitrogenous base –Phosphate group (PO 4 )

48. 4 nitrogenous bases;

49. Nucleic Acids Nitrogenous bases are complimentary A-T C-G Hydrogen bonds Sugar-phosphate backbone

52. H bonding

54. Relationship between nucleic acids and proteins