1. List a Carbohydrate Monomer
List a Carbohydrate Polymer
List a Lipid Monomer
List a Lipid Polymer

2. Organic Compound Quiz

3. 11. Hydrogen bonds can form between regions of polar molecules that are
a. nonpolar.
b. negatively charged.
c. oppositely charged.
d. uncharged (neutral).
12. An ion is formed when an atom gains or loses
a. protons.
b. neutrons.
c. bonds.
d. electrons.

4. 2.3 Carbon Based Molecules
Chemistry of Life
2.3 Carbon Based Molecules

6. Properties of
Carbon
Carbon forms covalent bonds with up to four other atoms, including other carbon atoms.

7. Monomer – Small molecule that is a single unit in a much larger molecule.
Polymer –Large molecule (macromolecule) formed from many monomers bonded together.

8. Is it a Monomer or Polymer?

9. Carbohydrate Type of Molecule Functions Monomers / Polymers
Broken down to
provide a source of energy
Make up plant cell walls
Carbohydrate
Monomer – Glucose
Polymer – Starch
– Cellulose

11. Glucose

12. Lipid Type of Molecule Functions Monomers / Polymers – Triglyceride
Broken down to
provide a source of energy
Make up
cell membranes
– Triglyceride
– Phospholipid
Glycerol + Fatty Acid
Lipid

13. Proteins Type of Molecule Functions Monomers / Polymers Enzymes
Transport oxygen
muscle movement
Proteins

14. GENERAL CHARACTERISTICS AND IMPORTANCES:
• Polymers of amino acids
• Each has unique 3-D shape
• Vary in sequence of amino acids
• Major component of cell parts
• Provide support
• Storage of amino acids
• Receptor proteins; contractile proteins; antibodies; enzymes

15. BUILDING BLOCKS:
Amino acids
20 different amino acids

17. PEPTIDE BONDS:

18. PROTEIN CONFORMATION:
Unique 3-D shape
PRIMARY:
Sequence of amino acids
Determined by genes
(sequence of bases in DNA)
SECONDARY:
Regular repeated folding of
peptide chain
Folding stabilized by hydrogen
bonds
b pleated sheet
a helix
TERTIARY:
Globular proteins
Irregular contortion
Shape stabilized by H bonds, ionic bonds,
hydrophobic interactions, disulfide bridges
Enzymes
QUATERNARY:
Interaction of several Polypeptides
Hemoglobin
Collagen

19. Protein Lab
Construct a protein with the following Amino Acid sequence.
1 green white yellow white green
Primary structure

20. Protein Lab
Now fold the protein so that the polar regions interact with polar regions and nonpolar with nonpolar.
Secondary structure

21. Protein Lab Now bond the two green amino acids together.
Tertiary structure

22. DENATURATION: Changing protein’s shape
Change shape = change in activity
How?
1. High temperature
2. Chemical agent (acid or base) change in pH
3. Organic solvent

23. DNA & RNA Store Genetic Information Build Proteins Type of Molecule
Functions
Monomers / Polymers
Nucleic Acids
Store Genetic Information
Build Proteins
DNA & RNA
Monomer – Nucleotide
Polymer – DNA and RNA

24. Fatty acids and Glycerol
CFA Quiz Standard 1.h
Organic Compound
List the monomer
List a polymer #1 #2
Protein
(Ex. Hemoglobin)
Nucleic Acid #3 #4 #5
Fatty acids and Glycerol #6 #7 #8
Glycogen, Starch

25. What elements do Carbohydrates have?
What is a main function of Proteins?

26. Fatty acids and Glycerol
CFA Quiz Standard 1.h
Organic Compound
List the monomer
List a polymer #1
PROTEIN #2
AMINO ACID
Protein
(Ex. Hemoglobin)
Nucleic Acid #3
NUCLEOTIDE #4
DNA / RNA #5
LIPID
Fatty acids and Glycerol #6
TRIGLYCERIDE
PHOSPHOLIPID #7
CARBOHYDRATE #8
GLUCOSE / STARCH
Glycogen, Starch

27. What elements do Carbohydrates have?
C H O
What is a main function of Proteins?
ENZYME / TRANSPORT OXYGEN /MUSCLE

28. Enzymes

29. ENZYME PROPERTIES & STRUCTURE
Globular proteins
Catalysts - speed up chemical rxns by lowering activation energy (energy needed to start rxn)
Not used up in chemical rxn
Active site = groove or pocket where substrate binds
Specific
Shape related to function – change shape (denature) enzyme no longer functions
Yellow = active site
Pink = enzyme

30. ENZYME ACTION – INDUCED FIT MODEL
Enzyme = pink
Active site = Yellow
Substrate = red
Substrate binds
to enzyme at active site
Enzyme (active site) changes
Shape
Bonds form between substrate (or break)
Product (green)
Released
Enzyme
unchanged &
ready to be used
again

32. CFA Quiz 1.h 1) What are enzymes made out of?
2) How do enzymes speed up chemical reactions?
3) What is the optimal temperature for the enzyme represented in the graph?
4) What affect can too high of temperature have on an enzyme?