1. Lipids

2.  A class of molecules that is hydrophobic  Hydrophobic= water fearing Ex.  Fats  Oils  Steroids

3. Fat  Made up of Glycerol and fatty acids  Glycerol-3 carbon backbone  Fatty acid= long hydrocarbon chain Glycerol Fatty acid

4. Saturated Fat  Saturated Fat= a fat that has all three fatty acid chains contain the maximum number of hydrogen atoms  Only single bonds  Found in most animal fat Lard butter

5. Saturated Fat

6. Unsaturated Fat  Unsaturated Fat= A fat that has less than the maximum number of hydrogen's bonded.  Some Carbon atoms are double bonded. Corn Oil Olive Oil Vegetable oil

7. Unsaturated Fat

8. Steroids  Steroid= a lipid molecule made up of four fused rings  Are lipids because they are hydrophobic  Chemical messenger Estrogen Testoterone

9. Steroids

10. Cholesterol  Cholesterol= an essential cell membrane lipid.  Starting point of steroids  Good and bad uses

11. Proteins

12. Protein  Protein= a polymer made up of amino acids  20 different amino acids  Uses Hair Muscles Nutrient storage

13. Amino Acids  Amino Acid= a monomer made up of a central carbon and four partners  Three are the same and one changes to create 20 different amino acids

14. Amino Acid Carboxyl (acid) group Amino group

15. Building Proteins  Proteins are made by connecting amino acids into a chain called a polypeptide  Each amino acid is linked by a dehydration reaction  Linked between the amino group and carboxyl group

16. Building a Protein Amino acid Dipeptide Amino acid Peptide bond Dehydration reaction Amino group Carboxyl group

17. Protein Shape  A protein consists of one or more polypeptide precisely folded into a unique shape  The shape is influenced by the environment  Temperature and pH change will change the shape of a protein = denaturation

18. Protein Shape Levels of Protein Structure Amino acids Basic structure of protein is a long chain of amino acids.

19. Secondary Shape  Secondary Shape folds the amino acid chain into two shapes Alpha Helix Beta Pleated Sheet

20. Secondary Shape Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet

21. Tertiary Shape  Brings multiple polypeptides together and continues to fold them

22. LE 3-14c Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet Polypeptide (single subunit of transthyretin)

23. Quaternary Shape  Multiple polypeptides are folded together into a useable shape held together by hydrogen bonds

24. LE 3-14d Levels of Protein Structure Amino acids Hydrogen bond Alpha helix Pleated sheet Polypeptide (single subunit of transthyretin) Transthyretin, with four identical polypeptide subunits

25. Enzymes

26. Catalyst  A compound that speeds up chemical reactions

27. Enzymes  A biological catalyst  A specialized protein that lowers the activation energy of chemical reactions

28. Activation Energy  Amount of energy needed to start a chemical reaction

29. Reactants Net change in energy E A without enzyme Products Progress of the reaction Energy E A with enzyme

30. Substrate Enzyme Active site Normal binding of substrate Enzyme

31. LE 5-6 Enzyme available with empty active site Active site Glucose Fructose Products are released Enzyme (sucrase) Substrate (sucrose) H2OH2O Substrate is converted to products Substrate binds to enzyme with induced fit

32. b. a. f. c. d. e.