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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.

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Presentation on theme: "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."— Presentation transcript:

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.

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

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

5 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

6 FIG 5.2 Condensation = builds longer molecules, H2O results Hydrolysis= breaks H2O bonds, shortens molecules

7 Carbohydrates mono-, di-, and polysaccharides CH 2 O (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)

8 Monosaccharides, Structural Isomers, (Aldoses, Ketoses)

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

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

11 Disaccharide: condensation (dehydration) Glycosidic linkages Sucrose = glucose + fructose

12 Lipids Hydrophobic “water fearing” Mainly hydrocarbons waxes, pigments, steroids, fats, phospholipids

13 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 http://www.mercola.com/2001/aug/1/oil.htm

14 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

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16 Phospholipid (cell membranes)

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18 Lipids: Steroids 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. cholesterol

19 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

20 Peptide bonds: condensation

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

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

23 http://www.expasy.ch/swissmod/gifs/GenomeResearchCoverSmall.gif

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

25 4 Levels of Protein Configuration 1. Primary: sequence of amino acids, as determined by DNA insulin, sickle cell anemia: evolution 2. Secondary: coils and/or folds, alpha helix, pleated sheets, **due to Hydrogen Bonds Important AP test concept!

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27 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)

28 Tertiary

29 9 non-polar amino acids: note the hydrocarbon groups

30 Tertiary

31 4. Quaternary: (not all proteins have the 4 th 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)

32 Collagen and Hemoglobin

33 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

34 REVIEW:

35 Denaturation then refolding (sometimes)

36 Nucleic acids: 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)

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39 Protein Synthesis

40 A few different movies with this chapter on the CD Rom

41 Steroid example: cholesterol


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