2. Students Will Be Able To: Compare and contrast the four biomacromolecules in terms of: Monomers, polymers, composition, examples, and primary functions in a cell. Identify a biomacromolecule given information about any of the comparative categories listed above.

3. Nucleic acids:  Information molecules  Contain H, O, N, C, and P  Monomers: Nucleotides Nucleotide has three parts  5 carbon sugar  Nucleic acid/nitrogenous base  phosphate group

4. Nucleic Acids  Function: genetic material  stores information  genes  blueprint for new cells  blueprint for next generation  transfers information  blueprint for building proteins  DNA  RNA  protein proteins

5. Nucleic Acids Examples DNA  Deoxyribonucleic Acid RNA  Ribonucleic Acid

6. Nucleic acids  Building block = nucleotides  5 different possible nucleotides  different nitrogen bases  A, T, C, G, U nucleotide – nucleotide – nucleotide – nucleotide phosphate sugar N base Nitrogen bases I’m the A,T,C,G or U part!

7. Nucleotide chains  Nucleic acids nucleotides chained into a polymer  DNA  double-sided  double helix  A, C, G, T  RNA  single-sided  A, C, G, U phosphate sugar N base phosphate sugar N base phosphate sugar N base phosphate sugar N base strong bonds

8. DNA  Double strand twists into a double helix weak bonds between nitrogen bases join the 2 strands  A pairs with T  A :: T  C pairs with G  C :: G the two strands can separate when our cells need to make copies of it

9. Proteins:  Highly diverse group  Elements: C, H, N, and O

10. Proteins  Function: many, many functions Structure & Movement  muscle Regulated chemical reactions and processes = enzymes  help chemical reactions Transport substances in and out of cells  part of cell membranes Pigments  skin color, melanin Hormones  signals from one body system to another  Insulin Immune system  protect against germs

11. Proteins insulin Examples muscle skin, hair, fingernails, claws  collagen, keratin pepsin  digestive enzyme in stomach insulin  hormone that controls blood sugar levels pepsin

12. Proteins  Building block =  In a condensation reaction, two amino acids form a covalent bond, called a peptide bond. Two amino acids bond to form a dipeptide. A very long chain of amino acids is called a polypeptide. amino acid amino acid – amino acid – amino acid – amino acid – amino acids

13. Amino acid chains  Proteins amino acids chained into a polymer  Each amino acid is different Some hydrophilic, some hydrophobic Some positively charged, some negative, some neutral Some polar, some nonpolar amino acid

14. Water-fearing amino acids  Hydrophobic “water fearing” amino acids try to get away from water in cell  the protein folds

15. Water-loving amino acids  Hydrophilic “water loving” amino acids try to stay in water in cell  the protein folds

16. Its shape that matters!  Proteins fold & twist into 3-D shape  Different shapes = different jobs  Proteins do their jobs, because of their shape  Unfolding a protein destroys its shape wrong shape = can’t do its job unfolding proteins = “denature”  temperature  pH (acidity) folded unfolded “denatured”

17. Students Will Be Able To: Explain how enzymes function as biological catalysts, in terms of activation energy and the lock and key model. Use a diagram/model of enzyme action to identify the enzyme, substrate, enzyme-substrate complex, product, and active site. Explain the effects of temperature, pH, and concentration on enzyme action.

18. Enzymes are proteins  Each enzyme is the specific helper to a specific reaction each enzyme needs to be the right shape for the job enzymes are named for the reaction they help  sucrase breaks down sucrose  proteases breakdown proteins  lipases breakdown lipids  DNA polymerase builds DNA

19. Nothing works without enzymes!  How important are enzymes? all chemical reactions in living organisms require enzymes to work  building molecules  synthesis enzymes  breaking down molecules  digestive enzymes enzymes speed up reactions  “catalysts”  Remind me, how do they do that? ++ enzyme

20. Enzymes aren’t used up  Enzymes are not changed by the reaction used only temporarily re-used again for the same reaction with other molecules very little enzyme needed to help in many reactions enzyme substrateproduct active site

21. It’s shape that matters!  Lock & Key model shape of protein allows enzyme & substrate to fit specific enzyme for each specific reaction

22. Reactants bind to the enzyme at the active site. Chemical reaction changes reactants to products. Product is released. Enzyme is available again. Enzyme Action

23. Enzyme vocabulary  Substrate: reactant in an enzyme- catalyzed reaction  Enzyme-substrate complex: enzyme & substrate temporarily joined during the time of the reaction  Active site: part of enzyme that substrate molecule fits into

24. What affects enzyme action  Temperature why? enzyme has to be right shape  pH (acids & bases) why? enzyme has to be right shape If enzyme is the wrong shape, why won’t it work?

25. Temperature  Effect on rates of enzyme activity Optimum temperature  greatest number of collisions between enzyme & substrate  human enzymes =  35°- 40°C (body temp = 37°C) Raise temperature  denature protein = unfold = lose shape Lower temperature  molecules move slower, decreases collisions

26. pH  Effect on rates of enzyme activity pH changes protein shape most human enzymes require neutral pH (6-8)  But it depends on where in body  pepsin (stomach) = pH 3  trypsin (small intestines) = pH 8

27. A change in the enzyme prevents reactants from binding. Shapes don’t match. Chemical reaction can’t occur. Reactants don’t get changed to products. Effects of Altered pH or Temperature on Enzyme Action

28. Enzyme concentration  Effect on rates of enzyme activity as increase amount of enzyme = increases how fast the reaction happens, up to a point  more enzymes = more frequently they collide with substrate

29. Substrate concentration  Effect on rates of enzyme activity as increase amount of substrate = increases how fast the reaction happens, up to a point  more substrate = more frequently they collide with enzyme