1. AP Biology MOLECULE PROPERTIES  How does chemistry play a foundational role in biology?  What properties of water make it so vital to living organisms?  Why does carbon play a central role in all living organisms?  What are the main types of molecules that form the basis of all living organisms?  Eight allotropes of carbon: a) Diamond, b) Graphite, c) Lonsdaleite, d) C60 (Buckminsterfullerene or buckyball), e) C540, f) C70, g) Amorphous carbon, and h) single-walled carbon nanotube or buckytube.carbonDiamondGraphiteLonsdaleiteBuckminsterfullerenebuckyballAmorphous carboncarbon nanotubebuckytube

2. AP Biology Proteins

3. AP Biology 2006-2007 Proteins Multipurpose molecules

4. AP Biology Proteins  Most structurally & functionally diverse group of biomolecules  Function:  involved in almost everything  enzymes (pepsin, polymerase, etc.)  structure (keratin, collagen)  carriers & transport (membrane channels)  receptors & binding (defense: antibodies)  contraction (actin & myosin)  signaling (hormones: insulin)  storage (bean seed proteins)

5. AP Biology Proteins  Structure:  monomer = amino acids  20 different amino acids  polymer = polypeptide  protein can be one or more polypeptide chains folded & bonded together  large & complex molecules  complex 3-D shape Rubisco hemoglobin growth hormones

6. AP Biology Amino acids  Structure:  central carbon  amino group  carboxyl group (acid)  R group (side chain)  variable group  confers unique chemical properties of the amino acid —N——N— H H C—OH || O R | —C— | H

7. AP Biology Nonpolar amino acids  nonpolar & hydrophobic Why are these nonpolar & hydrophobic?

8. AP Biology Polar amino acids  polar or charged & hydrophilic Why are these polar & hydrophillic?

9. AP Biology Ionizing in cellular waters H+ donors

10. AP Biology Ionizing in cellular waters H+ acceptors

11. AP Biology Sulfur containing amino acids  Form disulfide bridges  cross links betweens sulfurs in amino acids You wondered why perms smelled like rotten eggs? H-S – S-H

12. AP Biology Building proteins  Peptide bonds  linking NH 2 of one amino acid to COOH of another  C–N bond peptide bond dehydration synthesis

13. AP Biology Building proteins  Polypeptide chains  N-terminus = NH 2 end  C-terminus = COOH end  repeated sequence (N-C-C) is the polypeptide backbone  can only grow in one direction

14. AP Biology Protein structure & function hemoglobin  Function depends on structure  3-D structure  twisted, folded, coiled into unique shape collagen pepsin

15. AP Biology Primary (1°) structure  Order of amino acids in chain  amino acid sequence determined by gene (DNA)  slight change in amino acid sequence can affect protein’s structure & it’s function  Just one amino acid change can make all the difference!  What type of bonds are created between amino acids? lysozyme: enzyme in tears & mucus that kills bacteria

16. AP Biology Sickle cell anemia

17. AP Biology Secondary (2°) structure  “Local folding”  folding along short sections of polypeptide  interaction between adjacent amino acids  H bonds between R groups   -helix   -pleated sheet

18. AP Biology Secondary (2°) structure

19. AP Biology Tertiary (3°) structure  “Whole molecule folding”  determined by interactions between R groups  hydrophobic interactions  effect of water in cell  anchored by disulfide bridges (H & ionic bonds)

20. AP Biology Quaternary (4°) structure  More than one polypeptide chain joined together  only then is it a functional protein  hydrophobic interactions hemoglobin collagen = skin & tendons “Let’s go to the video tape!” (play movie here)

21. AP Biology Protein structure (review) 1° 2° 3° 4° aa sequence peptide bonds R groups H bonds R groups hydrophobic interactions, disulfide bridges determined by DNA multiple polypeptides hydrophobic interactions

22. AP Biology Denature a protein  Unfolding a protein  disrupt 3° structure  pH  salt  temperature  unravels or denatures protein  disrupts H bonds, ionic bonds & disulfide bridges  destroys functionality  Some proteins can return to their functional shape after denaturation, many cannot In Biology, size doesn’t matter, SHAPE matters!

23. AP Biology Chaperonin proteins  Guide protein folding  provide shelter for folding polypeptides  keep the new protein segregated from cytoplasmic influences

24. AP Biology Protein models  Protein structure visualized by  X-ray crystallography  extrapolating from amino acid sequence  computer modelling lysozyme

25. AP Biology 2006-2007 Let’s build some Proteins!