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Unit 1: The Chemistry of Life

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1. State the empirical formula for a carbohydrate. Explain what ... c. 2 sulfhydryl groups can form a disulfide bridge. d. charged R groups can attract or repel ... – PowerPoint PPT presentation

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Title: Unit 1: The Chemistry of Life


1
Unit 1 The Chemistry of Life
  • Chapter 5
  • Macromolecules

2
Macromolecule theme
  • Monomers
  • Polymers

3
1. State the empirical formula for a
carbohydrate. Explain what such a formula means.
  • (CH2O)n Carbon, Hydrogen, Oxygen
  • Mostly we study the 6-carbons sugars
  • Rings, not chains
  • Recognize as dietary sugars, but have other uses

4
2. To what do the terms monosaccharide,
disaccharide, and polysaccharide refer? What do
all three have in common?
  • mono - one
  • di two
  • oligo several (mainly cell surfaces)
  • poly many
  • All levels have the same formula (CH2O)n

5
3. Explain what is meant by dehydration
synthesis. What is the opposite process called?
How are both important to most biological
molecules?
  • Dehydration loss of water synthesis to make
  • Make a molecule by dehydrating it
  • Hydro water Lysis to break apart
  • Using water to break apart molecules
  • Both require specific enzymes
  • To live, we must build up molecules, and tear
    molecules down
  • EX Eating carbos / waking up

6
4. List the important differences between
starches and glycogen. Where would each be found?
  • Starches ? string of glucoses
  • somewhat branched
  • form storage granules in PLANTS
  • Glycogen? string of glucoses
  • highly branched
  • energy storage for animals (Fungi too)
  • found in the liver muscles

7
5. What is it that makes cellulose strong? How
is its strength further increased in plant fibers?
  • Its arrangement makes cellulose strong
  • Beta linkages create a sturdy, rigid structure
  • Hydrogen bonding then forms long, microfibrils
    like a suspension bridge
  • Forms sturdy cell walls in plants
  • Cellulose is dietary fiber we cant digest
    any of it, but its important to eat. Why?
  • - We dont have the enzyme to break the linkage!
  • How do cattle, deer, goats, etc. digest it?
  • They house microorganisms to do it (4 stomachs)

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9
6. What is the role of chitin and how is it
different from other carbohydrates?
  • Chitinexoskeleton of insects arthropods
  • Very soft, but when combined w/ CaCO3, becomes
    very hard
  • Where does the CaCO3 come from?
  • Water

10
  • 7. List the essential parts of a triglyceride.
  • 1 glycerol and 3 fatty acid molecules
  • Through what enzymatic process are triglycerides
    joined?
  • Dehydration synthesis
  • What makes one triglyceride differ from the
    next?
  • Length of fatty acid chain, degree of saturation
  • Which end of the triglyceride is more
    hydrophobic?
  • The long chain portion.

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8. Distinguish between an oil and a fat and
between a saturated fat, an unsaturated fat, and
apolyunsaturated fat. Are unsaturated fats more
common in animal tissue? Explain.
  • Oil ? liquid at room temperature
  • Fat ? solid at room temperature
  • Saturated ? C-C single bonds, most Hs
  • Ex. Lard, steak fat
  • Unsaturated ? CC, fewer Hs
  • Ex. Olive oil
  • Polyunsaturated ? many CCs
  • Sat. Fat more common in animal tissue
  • Need to be solid at normal temps!

13
9. Describe the general structure of
phospholipids, and explain their arrangement into
membranes.
  • Phosphate head (Hydrophilic)
  • 2 fatty acid chain tails (Hydrophobic)
  • One is saturated, one is not

14
By a diagram of a phospholipid bilayer, indicate
the hydrophobic and hydrophilic regions.
15
10. List the special uses of steroids. How do
steroids differ structurally from other lipids?
  • Steroids ? structurally different from fatty
    acids or lipids
  • They hate water thats why theyre lipids!
  • 4 linked carbon rings
  • Examples
  • lanolin ? sheeps wool, human hair
  • cholesterol ? in cell membrane, sex hormones
  • Allow flexibility in hair / membranes

16
Cholesterol
17
11. What are six significant uses for proteins?
  • Enzymes ? reactions
  • Energy ? although not preferred
  • Immunity ? antibodies
  • Structure / Support ? muscle, tendon, etc.
  • Hormones ? insulin, epinephrine, prolactin
  • Carriers ? hemoglobin carries O2

18
12. Carefully define the term protein. How is a
protein different from a polypeptide?
  • Proteins? large, complex molecules made up of
    amino acids joined by dehydration synthesis
    reactions
  • Polypeptide ?a string of A.A.s
  • transported in blood like this
  • cells take p.p.s in and utilize the A.A.s

19
13. What do all amino acids have in common? How
do they differ?
  • Each A.A. has a carbon with four groups
  • amine group (NH2)
  • carboxyl group (COOH)
  • Hydrogen
  • R group

How many A.A.s? How many are essential?
20
14. Describe the four levels of organization
possible in a protein, and explain what forces
are involved at each level.
  • Primary ? sequence of amino acids
  • sequence will determine future shape

21
Secondary
  • Secondary? segments of the polypeptide fold and
    coil in patterns
  • alpha helices
  • beta sheets
  • What forces?
  • H-Bonds

22
Tertiary
  • Tertiary? bends and twists cause a three
    dimensional shape. Why?
  • a. nonpolar R groups group together away from
    the polypeptide
  • b. H-bonds can form between polar R groups
  • c. 2 sulfhydryl groups can form a disulfide
    bridge
  • d. charged R groups can attract or repel

23
Quaternary
  • Quaternary ? two or more polypeptide chains
    interacting w/ each other
  • same forces as tertiary

24
15. How do collagen and hemoglobin differ in
reference to size, shape and function?
25
16. What is the process which links two amino
acids together? Describe the reaction.
  • Dehydration Synthesis
  • But you knew that!!!!

26
17. What is denaturation? How or when may it
occur? What does a protein lose when it becomes
denatured?
  • Denaturation? when a protein unravels or loses
    its shape (becomes inactive)
  • -normally a polypeptide will spontaneously
    arrange itself, however
  • Changes in
  • pH
  • salt concentration
  • temperature
  • other environmental aspects

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29
18. Identify the three types of monomers found in
a nucleotide.
  • 5-carbon sugar
  • Phosphate
  • Nitrogenous base
  • DNA RNA

30
19. Name which nitrogenous bases are purines.
Pyrimidines?
  • Purines Adenosine (A) Guanine (G)
  • Pyrimidines Cytosine (C) Thymine (T)
  • Hint? Y do you ask?

31
20. How are purines and pyrimidines linked in a
double helix? Which ones attach to which?
  • Linked by hydrogen bonds
  • A T
  • G C

32
Whats the monomer or polymer in..
  • Cellulose
  • A polypeptide
  • DNA
  • Glucose
  • Sucrose
  • Amino acid
  • Trigylceride
  • Starch
  • Cholesterol
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