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 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

8. AP Biology Polar amino acids  polar or charged & hydrophilic

9. 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

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

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

12. 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  even just one amino acid change can make all the difference! lysozyme: enzyme in tears & mucus that kills bacteria

13. AP Biology Sickle cell anemia

14. 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

15. 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)

16. 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

17. AP Biology Protein structure (review) 1°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

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

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

20. AP Biology 2006-2007 Any Questions??