Chemistry

1. Chemistry Macromolecules

2. Macromolecules • Small molecules linked together to create large molecules • Have shape created by hydrogen bonding, sulfhydryl bonding, polarity, etc. • FORM FITS FUNCTION • Ex. Proteins do ‘everything’

3. Protein

4. Linus Pauling Stanley Miller

5. Carbon bonds 4 times in multiple ways Creates great variety

6. Hydrocarbons

7. ISOMER

8. Isomers= molecules with the same formula but different structural formulae; not isotope

9. GTP AMP ATP

10. Differences in functional groups What is a functional group?

12. Ethane Functional group Ethanol

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

14. Dehydration synthesis = enzymatically controlled formation of large molecules by removal of water

15. Macromolecules • Monomers + monomers + monomers = polymers • Produced by DEHYDRATION SYNTHESIS • Hydrolysis – breakdown of macromolecules by the addition of water • Enzymes

16. Macromolecules • What do you need to know for each macromolecule important to life: • Structure • Monomers • Function in organisms

17. Macromolecules • Carbohydrates • Lipids • Proteins • Nucleic acids

18. Carbohydrates • Carbon + water (hydrate) • Basic formula: CH2O(n) • Monomers = monosaccharide (‘one sugar’) • End in ‘ose’

19. Monosaccharides • Glucose C6H12O6 • Many monomers form rings in aqueous solutions to become more stable • Monomers may be functional: • Glucose isprimary source of energy for organisms

20. Carbohydrates • Monomer + monomer = dimer • Monosaccharide + monosaccharide = disaccharide • Glucose + glucose = maltose • Glucose + fructose = sucrose • Glucose + galactose = lactose

21. Polysaccharides

22. Polysaccharides • Polymers of monosaccharides • Type of monosaccharide and arrangement creates variation in polysaccharides • Starch(Amylose, amylopectin)= plants • Glycogen= energy storage for animals • Cellulose= plant cell walls • Chitin= exoskeleton of arthropods, some fungi

24. Carbohydrates: Function • Energy; stored energy (which?) • Structure – (which?) • Cell-to-cell communication, identification (glycoproteins, glycolipids) • Antigens /antibodies

25. Lipids • Insoluble in water; (long, nonpolar hydrocarbon chains) • Basic formula: C50H70O6 • Three types: • Fats, oils, waxes • Phospholipids • Steroids

26. Lipids: Fats • Macromolecules of glycerol + 3 fatty acids • Glycerol = glyc = ‘sugar’ C3H8O3 • Fatty acids = hydrocarbon chain (16-18 carbons) • Hydrocarbon chain is hydrophobic

27. Lipids: Fats • Fats = triglycerides (3 fatty acids) • Structure of the fatty acid chains creates variety in types of fats • Saturated – full of hydrogen atoms; no double bonds • Unsaturated – not full; double bond(s)

29. Saturated No double bonds Saturated Solids @ (200) Animal fats Bacon grease, lard, butter Unsaturated Double bond(s) Unsaturated Liquids @ (200) Plant fats (oil) Corn, peanut, olive oils Types of Fats

30. Link between an acid and a sugar

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

32. Lipids: Phospholipids • Glycerol + 2 fatty acids • 3rd position on the glycerol is taken by a phosphate group (PO4)

33. Phospholipids • Major component of cell membrane • ‘head’ end (glycerol) is polar (term?) • Hydrophilic = “water loving” • ‘tail’ end is non-polar (term?) • Hydrophobic = “water fearing”

35. Phospholipids • Phospholipids in water form a micelle • First prokaryotes evolved when phospholipids formed micelles in water (?) • Abiogenesis

36. Steroids • 4 fused carbon rings + functional group • Insoluble in water • Ex. Cholesterol • Between fatty acids tails of phospholipids • Help to moderate the effects of extreme temperatures

38. Steroids • Precursors of sex hormones • Too much causes atherosclerosis (?)

39. Importance • Energy (?) • Padding (?) • Insulation (?) • Structure (?) • Hormones (?)

40. Proteins • Many shapes = many functions • ‘first place’ • Polymers of AMINO ACIDS • Linked by PEPTIDE BONDS • POLYPEPTIDES • Proteins = folded, shaped polypeptides

42. Proteins: Amino Acids • 2 carbon skeleton • Amino group • Carboxyl group • H atom • Side group (R group)

43. Proteins: Amino Acids • R group determines properties of the aa • Some are polar, some are nonpolar • Polar may be acidic or alkaline • 20 different amino acids • Essential = body cannot produce on its own

45. Proteins • Peptide bonds are the result ofdehydration synthesis • Amino group reacts with carboxyl group of adjacent amino acid • Polypeptide - string of polypeptide bonds

46. Proteins • Function depends upon shape • Conformation – 3d shape caused by H-bonds • Fold and twist the amino acids • Globular • Insulin, enzymes • Fibrous = ‘stringy’ • Silk, muscle

48. Proteins • Four levels of protein structure that give a protein its unique shape: • Primary • Secondary • Tertiary • Quaternary

49. Proteins: Primary Structure • Sequence of amino acids • Determined by genetic code • ‘goof’ in sequence can have harmful or lethal effects

50. Secondary Structure • Folds or twists created by H-bonding in the carbon backbone; NOT the R group • 2 types: both may be in a protein • Alpha - helix • Beta - pleated sheet