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Ch 5 Macromolecules

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The two enantiomers of Thalidomide can and do interact ... Peptide bonds: condensation. http://merlin.mbcr.bcm.tmc.edu:8001/bcd/ForAll/Media/1c2r.gif ... – PowerPoint PPT presentation

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Title: Ch 5 Macromolecules


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
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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
  • 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
  • CH2O (basic formula)
  • Carbonyl group (CO) Aldose vs Ketose
  • Glucose, galactose, and fructose (isomers), see
    next slide
  • Bodys 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. contd
  • 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
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 bodys organs, protection,
    insulation
  • Atherosclerosis, arterio., adipose cells
  • Saturated v. unsaturated ?
  • hydrogenated vegetable oils ?
    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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Phospholipid (cell membranes)
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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.

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.edu8001/bcd/ForAll/Med
    ia/1c2r.gif

22
  • http//abc.net.au/science/slab/genome2001/img/prot
    ein.jpg

23
  • http//www.expasy.ch/swissmod/gifs/GenomeResearchC
    overSmall.gif

24
http//gcg.tran.wau.nl/ccmv-overview/ccmv-icosa-pe
nta-hexa.jpeg
25
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!
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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 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)

32
Collagen and Hemoglobin
33
Proteins continued
  • Specific environmental needs pH, salt
    concentration, temperature, other environmental
    aspects (well see with enzymes - Ch.6)
  • Denaturation re-folding is sometimes possible
  • Chaperone proteins

34
REVIEW
35
Denaturation then refolding (sometimes)
36
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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