1. Chapter 5 Macromolecules Building blocks of life

2. Macromolecule Composition Monomers Polymer Covalent linkages Dehydration reactions Hydrolysis reactions

3. Categories of Macromolecules Carbohydrates Lipids Proteins Nucleic acids

4. Carbohydrates Sugars Sugar polymers Glycosidic linkage –Covalent Categories –Monosaccharide –Disaccharide –Polysaccharide

5. Monosaccharides Single sugar molecule Can function as monomer Ring form Aldoses Ketoses

6. Ring Forms of Sugars

7. Disaccharides Two sugar molecules Dehydration reaction Glycosidic bond Sucrose Lactose Maltose

8. Derivatives of Carbohydrates Sweeteners

9. Polysaccharides Many sugar molecules Glycosidic linkage Starch –Alpha Cellulose –Beta –Structural polysaccharide Chitin

10. Lipids Fats and oils Hydrocarbon tails or rings Very non polar No true monomer Most composed of glycerol and fatty acids Linkage-ester

11. Subcategories of Lipids Neutral lipids Phospholipids Steroids Waxes

12. Neutral Lipids Glycerol backbone 1, 2, or 3 fatty acids Triglyceride Ester linkage Adipose storage Plant oils Saturated- animal source Unsaturated- plant source

13. Phospholipids Glycerol backbone 2 fatty acid tails Phosphate head Amphipathic Polar head Non-polar tails Components of all biological membranes

14. Phospholipids (cont.) Bilayer Micelle Liposome Emulsifying agent

15. Steroids Common ring structure Very planar Sex hormones Cholesterol –Stabilize membranes

16. Waxes Very hydrophobic Long chain alcohol esterified to very long chain fatty acid Waterproofing Ducks

17. Proteins Polymers of amino acids Amino acid as monomer Peptide bonds Very diverse group of macromolecules

18. Amino Acids

20. Essential Amino Acids Animal sources Plant sources –Complementation groups

21. Protein functions Enzymatic proteins Structural proteins Storage proteins Transport proteins Hormonal proteins Receptor proteins Contractile and motor proteins Defensive proteins

22. Enzymatic Proteins Catalyst Rate of reactions Energy changes “Match maker” Shape Active site Activation energy

23. Structural Proteins Confer shape Capsid proteins Cytoskeletal proteins

24. Storage Proteins Albumin Amino acid storage Egg white

25. Transport Proteins

26. Receptor protein Hormones Viruses Cell communication

27. Contractile Proteins

28. Defense Proteins Antibodies

29. Protein Structure Four levels of organization Primary Secondary Tertiary Quaternary See pages 82-83 in text

30. Primary and Secondary

31. Tertiary and Quaternary

32. Denaturation Unfolding Break H bonds Heat pH changes

33. Protein Folding Hydrophilic interactions H bonding S-S bridges Chaparonins

34. Amino Acid Sequence Ultimately determined by the DNA base sequence Dictates final folding and shape

35. Nucleic Acids Polymers of nucleotides DNA RNA

36. Nucleotides 5 carbon sugar –Ribose –Deoxyribose Nitrogenous base –Adenine –Guanine –Cytosine –Thymine –Uracil Phosphate- 1, 2, or 3

37. Nitrogenous base Letters in genetic code Purines –Adenine –Guanine Pyrimidines –Thymine –Cytosine –Uracil

38. Structure of Nucleic acids Sugar/ Phosphate back bone- similar to paper N base as “letter” written on the backbone Anti-parallel alignment if double stranded

39. Functions of Nucleic Acids Information molecules DNA –Hereditary information –Recipe book –Each recipe is one gene –Each gene encodes one protein RNA –Working copy of one gene or recipe

40. DNA Hereditary function –DNA replication Master recipe book –Transcription

41. RNA Working copy of a gene Transcription –Make RNA Translation –Make protein