CHAPTER 3 MACROMOLECULES

I. Functional groups in organic compounds

A. attached to C atoms
B. are most often involved in chemical
reactions
C. presence gives molecules unique properties
D. amino acid as example

Students responsible for 7 functional groups - be able to name,

recognize and describe them. See fig. 3.1

II. Isomers
A. compounds that have the same molecular formulas, but dif.
structures, and therefore dif. properties. 2 types:
1. structural - differ in arrangement of atoms
2. optical – mirror images of each other – often called
left and right ( L and D). Often only 1 or the other is
biologically active

III. Organic polymers

A. when small organic molecules (monomers) are
joined together – huge macromolecules (polymers)
are formed
B. 4 classes:

macromolecule (polymer) monomer

1. carbohydrates monosaccharide
2. lipids fatty acids
3. proteins amino acids
4. nucleic acids nucleotides
 C. condensation reaction: 2 monomers are linked
together by removing a water molecule
D. hydrolysis reaction: a polymer is broken down into
individual monomers by adding a water molecule
fig. 3.4
E. special helper proteins, called enzymes, are needed
for these reactions to take place.

IV. PROTEINS - C,H,N,O,S

A. most abundant macromolecule in the cell
B. structural, transport, hormonal functions
C. accelerate chemical reactions in cells in the form of
enzymes
D. proteins very diverse in living organisms, yet all
proteins (polymer) composed of various amts. and
proportions of same amino acids (monomer)
1. ≈20 dif. amino acids in all living things
2. amino acid structure:

table 3.2

3. amino acids are linked together by a peptide

bond (dehydration)
a. N and C terminus
b. partial charges

E. Levels of protein structure: fig. 3.7

1. primary - arrangement of amino acids linked by
peptide bonds
a. ultimately determines final shape
b. sequence of a.a.’s determined by genes
 2. secondary - α helix, β pleated sheet - due to
hydrogen bonds

3. tertiary - resulting from various bonding

between R groups - ionic, hydrophobic, van der
Waals, and disulfide bridges.
4. quaternary - two or more peptide chains
held together in one functional unit

F. shape = function
1. denaturation
2. chaperonins

V. Carbohydrates ≈CH2O
A. function in short-term energy, cellular structures
B. monosaccharides –
1. one monomer containing 3 - 7 Cs each
2. many are structural or geometric isomers of
each other
3. pentoses
4. glucose, fructose, galactose (6 Cs)
a. forms of glucose:

C. disaccharides
1. condensation makes glycosidic linkage

2. glu + fru = sucrose (table sugar)

3. glu + gal = lactose
4. glu + glu = maltose
 D. polysaccharides
1. huge polymer consisting of hundreds to 1000s
of monosaccharides
2. monomer is usu. glucose
3. examples of polysaccharides:
a. starch
b. glycogen
c. cellulose
E. modified carbohydrates
1. glucosamine and galactosamine
2. chitin

VI. Lipids
A. consist of mainly C and H, a few O
B. nonpolar (hydrophobic)
C. types of lipids:
1. fats: glycerol + 3 fatty acids
a. saturated - no double bonds

b. unsaturated - double bonds

2. phospholipids fig. 3.20

a. polar and nonpolar regions
b. major component of plasma
membranes

3. carotenoids
4. steroids - ringed structure:
5. vitamins
6. waxes
VII. Nucleic acids – DNA, RNA C,H,N,O,P
A. DNA
1. makes up chromosomes, genes
2. DNA is converted to RNA, which is then translated
into a particular protein.
3. replicated prior to cell division
4. sequences compared to establish evolutionary
relationships b/t organisms
B. RNA
1. synthesized from DNA
2. specifies the a.a sequence in a protein
3. makes peptide bonds b/t a.a. in ribosomes –
ribozymes

C. nucleic acids (polymer) made up of many

nucleotides (monomer)
1. structure: fig. 3.24
a. pentose sugar – ribose, deoxyribose
b. nitrogenous base – A, T, G, C, U
c. phosphate group
2. linked together by pentose and phos.
D. some nucleotides are not hooked together to make
nucleic acids:
1. ATP - adenosine triphosphate fig. 6.5
2. NADH, NADPH fig. 7.4

VI. Life’s origins

A. extraterrestrial
1. evidence

B. chemical evolution
 1. Miller-Urey experiment
2. refinements
3. polymerization of monomers
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OBJECTIVES FOR CHAPTER 3

1. Define condensation and hydrolysis

2. Know the monomers that make up proteins, lipids, carbohydrates, and nucleic acids
3. Define and describe the three polysaccharides, and know what monomers are put together to
build them.
4. Know the function of the various carbohydrates presented
5. Know the function of the various lipids presented
6. Distinguish between saturated and unsaturated fatty acids
7. Know the structure and function of phospholipids and steroids
8. Define enzyme
9. Describe the 4 levels of protein structure and what types of bonds are involved in each.
10. Define peptide bond, R group
11. Define denaturation and what causes it. Understand the relationship between protein shape
and function.
12. Know what type of molecule ATP and NADH are, and their biological importance.
13. Give examples of nucleic acids and their functions
14. Know the types of atoms each of the macromolecules is made of
15. Describe hypotheses on the origin of macromolecules
16. Be able to name and recognize the 7 functional groups presented in this chapter, and if any of
the 7 are acidic or basic.
17. Do Self-Quiz questions 1-6, 8-10
 SAMPLE QUESTIONS FOR CHAPTER 3

1. The sequence of amino acids in a polypeptide chain determine

a. primary structure of carbohydrates
b. primary structure of proteins
c. primary structure of ions
d. isotope formation
e. ionic formation

2. Proteins capable of speeding up specific chemical reactions are called

a. enzymes
b. peptides
c. messengers
d. ions
e. compounds

3. Which of the following are major components of cell membranes?

a. carbohydrates
b. phospholipids
c. nucleic acids
d. fatty acids
e. sterols

4. Most plant oils are

a. liquid at room temperature
b. unsaturated
c. solid at room temperature
d. saturated
e. a and b only

5. Genetic material is made up of primarily

a. proteins
b. polysaccharides
c. triglycerides
d. lipids
e. DNA

6. The cell walls of plants are composed of

a. cellulose
b. starch
c. glycogen
d. hemoglobin
e. chitin
7. ATP is an example of
a. a protein
b. a carbohydrate
c. a lipid
d. a nucleic acid
e. a nucleotide

8. When egg white, a protein, is heated, it changes its structure from liquid to solid. The
protein
is said to be _____________ by the heat.
a. hydrolyzed
b. denatured
c. transmogrified
d. disfunctionalized
e. condensed

9. Which of the following atoms is NOT found in nucleic acids?

a. C
b. H
c. N
d. O
e. S

10. The secondary structure of a protein

a. could be an α-helix
b. could be a β-pleated sheet
c. is held together by hydrogen bonds
d. is made up of amino acids
e. all of the above

11. Carbon can form covalent bonds with how many other atoms?
a. one d. four
b. two e. five
c. three