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The two enantiomers of Thalidomide can and do interact metabolically different.

The two enantiomers of Thalidomide can and do interact metabolically different. In the case of Thalidomide, it was discovered that only one of the two enantiomeric forms was responsible for the mutagenic effects seen. Chapter 5 The Structure and Function of Macromolecules.

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The two enantiomers of Thalidomide can and do interact metabolically different.

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  1. The two enantiomers of Thalidomide can and do interact metabolically different. In the case of Thalidomide, it was discovered that only one of the two enantiomeric forms was responsible for the mutagenic effects seen.

  2. Chapter 5The Structure and Function of Macromolecules Polymers: carbohydrates lipids proteins nucleic acids Their structures, sources, uses

  3. Polymers • polys (many) meris (parts) • Built of monomers (single units) • monosaccharides • Amino acids • Nucleotides

  4. Condensation (Dehydration) reaction:builds polymers (ex. on next slide) a water molecule is “made”(-H) (-OH) from the site where to two bond. • Hydrolysis: breaks polymers are disassembled hydro (water) lysis (break) water is broken (-H) (-OH) to fill the “gaps” left when the two parts separate • See fig. 5.2

  5. Condensation= builds longer molecules, H2O results Hydrolysis= breaks H2O bonds, shortens molecules • FIG 5.2

  6. Carbohydrates • mono-, di-, and polysaccharides • CH2O (basic formula) • Carbonyl group (C=O) Aldose vs Ketose • Glucose, galactose, and fructose (isomers), see next slide • Body’s uses: cellular respiration fuel, building blocks • Glycosidic linkage (the bond between monosaccharides to make di- and polysaccharides) (condensation)

  7. Monosaccharides, Structural Isomers, (Aldoses, Ketoses)

  8. Carbos. cont’d • Polysac-charides • Starch,glycogen, cellulose (cows), chitin, fungi • See alsoFig 5.6 Starch and cellulose Fig 5.7 NAME SOME COMMON SOURCES OF CARBOS IN OUR DIET

  9. I Love Carbs! • www.dietsearch.com/pasta/ http://www.oneworld.net/penguin/ food/food1.html

  10. Disaccharide: condensation (dehydration) • Glycosidic linkages • Sucrose = glucose + fructose

  11. Lipids • Hydrophobic “water fearing” • Mainly hydrocarbons • waxes, pigments, steroids, fats, phospholipids

  12. Lipids: FATS • Typical Fats = glycerol head and 3 fatty acid tails Fig5.10 • Uses: High energy storage (long term fuel), cushions the body’s organs, protection, insulation • Atherosclerosis, arterio., adipose cells • Saturated v. unsaturated ? • “hydrogenated vegetable oils” ? http://www.mercola.com/2001/aug/1/oil.htm

  13. Lipids: Phospholipids • Only 2 fatty acid tails and 1 phosphate group (negatively charged) • Tails are hydrophobic, phosphates are hydrophilic (water loving) • micelle, phospholipid bilayer • Selective: Cell membranes, brain tissue

  14. Phospholipid (cell membranes)

  15. Lipids: Steroids cholesterol Four fused rings (see fig 5.14) • Cholesterol (fig 4.8) and sex hormones • ** not made of polymers ! ** these are single units composed of 4 rings, they cannot be broken into smaller units.

  16. Proteins (peptides) • Proteios (first place) • For: Structural support, transport, signaling in the body, movement and defense against foreign substances, enzymes • 20 amino acids, polypeptide chains • Fig 5.15, amino group, carboxyl group • Peptide bonds (condensation reaction) to build proteins

  17. Peptide bonds: condensation

  18. http://merlin.mbcr.bcm.tmc.edu:8001/bcd/ForAll/Media/1c2r.gifhttp://merlin.mbcr.bcm.tmc.edu:8001/bcd/ForAll/Media/1c2r.gif

  19. http://abc.net.au/science/slab/genome2001/img/protein.jpg

  20. http://www.expasy.ch/swissmod/gifs/GenomeResearchCoverSmall.gifhttp://www.expasy.ch/swissmod/gifs/GenomeResearchCoverSmall.gif

  21. http://gcg.tran.wau.nl/ccmv-overview/ccmv-icosa-penta-hexa.jpeghttp://gcg.tran.wau.nl/ccmv-overview/ccmv-icosa-penta-hexa.jpeg

  22. 4 Levels of Protein Configuration • 1. Primary: sequence of amino acids, as determined by DNAinsulin, sickle cell anemia: evolution • 2. Secondary: coils and/or folds, alpha helix, pleated sheets, **due to Hydrogen Bonds Important AP test concept!

  23. Protein folding continued • 3. Tertiary: irregular contortions, bonding side chains (R-groups), hydrophobic interaction, van der Waals forces, Di-Sulfide bridges (sulfahydryl group on cysteine)

  24. Tertiary

  25. 9 non-polar amino acids: note the hydrocarbon groups

  26. Tertiary

  27. 4. Quaternary:(not all proteins have the 4th level of organization) overall structure that results from the aggregation of polypeptide units. Hooking more than one chain of polypeptides together (ex: hemoglobin, 4 parts)

  28. Collagen and Hemoglobin

  29. Proteins continued • Specific environmental needs: pH, salt concentration, temperature, other environmental aspects (we’ll see with enzymes - Ch.6) • Denaturation – re-folding is sometimes possible • Chaperone proteins

  30. REVIEW:

  31. Denaturation then refolding (sometimes)

  32. Nucleic acids: • DNA (cell division) double helix-1953 • RNA (protein synthesis) (ribosomes) • Genes • Know Figure 5.26, 5.27 !! • What is a Nucleotide? phosphate (negatively charged) sugar R(ribose, deoxyribose) base (pyrimidines C,T,U or purines A,G) • DNA as tape measures of evolution (Table 5.2)

  33. Protein Synthesis

  34. A few different movies with this chapter on the CD Rom

  35. Steroid example: cholesterol

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