College of St.
John - Roxas
MC 102 - Biochemistry
Name: _____________________________ Date Started-Completed: __________________________
Class: ____________ Group Number & Group Name: ______________________________________
Laboratory Activity 4
PROTEINS AND ENZYMES
A. Answer the following:
1. Define polypeptide.
2. Define protein.
3. What is the name of the individual units that make up the chain of polypeptides?
4. What is the name of the bond between these individual units?
5. How many different dipeptides can be made (a) using only alanine, tryptophan, glutamic acid, and arginine
and (b) using all 20 amino acids?
6. What is produced when a polypeptide chain is hydrolyzed?
7. Identify the monomers of protein.
8. Identify the polymers of protein.
9. Define amino acid.
B. In the space below, draw two simple amino acids hooked together by a peptide bond. Circle the
peptide bond.
C. For the following description, state which structure (or structures) best relates: primary 1o ,
secondary 2o, tertiary 3 o, quaternary 4 o. You may use more than one.
Description Structure
Alpha helix
Sequence of amino acids
found in fibrous protein
found in enzymes
maintained by hydrogen bonds
broken down only by hydrolysis (not denaturing)
found in silk
found only in globular proteins
broken down by denaturing
found in muscle
made of subunits of tertiary structure
D. Fill in the table below.
Amino Acids
Alanine ala
Arginine arg
asn
Aspartic acid
Cysteine
Glutamic acid
gln
gly
his
Isoleucine ile
Leucine leu
Lysine
Methionine
Phenylanine
pro
ser
Threonine thr
trp
Tyrosine
Valine
E. For the following, state if it best describes denaturing or hydrolysis
Description Denaturing or hydrolysis
losing the shape of the protein
happens when meat or eggs are cooked
loss of solubility
breaking the amide linkage
happens when a strong acid is added
loss of biological activity
when the chain is cut into individual amino acids
breaks hydrogen bonds
unfolds the protein
destroys primary structure
breaking of the polypeptide chain
F. Complete the following table by adding the function or type of protein
Type Function Examples
Enzymatic Proteins Selective acceleration Digestive enzymes catalyze the hydrolysis of
of chemical bonds in food molecules.
reactions.
Storage Proteins
Hormonal Proteins
Contractile and
Motor Proteins
Defensive Proteins
Transport Proteins
Receptor Proteins
Structural Proteins
G. Chemical Connections (from your Bettelheim book):
1. AGE products become disturbing only in elderly people, even though they also form in younger people.
Why don’t they harm younger people?
2. What does the reducing agent do in straightening curly hair?
3. Silver nitrate is sometimes put into the eyes of newborn infants as a preventive measure against
gonorrhea. Silver is a heavy metal. Explain how this treatment may work against bacteria.
4. Why do nurses and physicians use 70% alcohol to wipe the skin before giving injections?
5. Explain the difference in oxygen-binding behavior of myoglobin and hemoglobin.
6. How does the fiberscope help to heal bleeding ulcers?
7. How can a protein act as a buffer?
8. The cytochrome c protein is important in producing energy from food. It contains a heme surrounded by
a polypeptide chain. What kind of structure do these two entities form? To which group of proteins does
cytochrome c belong?
9. Hormones are molecules that are released from one tissue but have their effect in another tissue. Give an
example of a hormone you encountered that would be ineffective if taken orally.Give an example of one
that could be effective if taken orally
H. Enzymes
a) Fill in the gaps in the following sentences using the words in the box below.
i) Enzymes are biological ………………… that speed up chemical reactions in
living organisms.
ii) Enzymes are protein molecules, which are made up of long chains of ………...……….
iii) The sequence and type of amino acids are ………………… in each protein, so they produce
enzymes with many different shapes and functions.
iv) The shape of an enzyme is very important to its ………………….
different catalysts function the same amino acids
b) Enzymes catalyze many important chemical reactions in the human body. Name one of
these chemical reactions.
c) Label the image below with the following terms: active site, substrate, enzyme.
……………….....
………..….......
+ …….…...……
…..............
d) Enzymes and their substrates are often compared to a lock and key. This is called the Lock
and Key Model. Explain what it means.
e) Explain what would happen if a substrate molecule with a different shape to the enzyme
came into contact with the enzyme’s active site.
f) There are many factors that affect the rate of enzyme-catalyzed reactions, including
temperature. Name two other factors.
g) A group of students decided to carry out an investigation to find out how enzyme activity is
affected by temperature changes. They put samples of salivary amylase and starch into two
test tubes. Salivary amylase is an enzyme that breaks down starch into maltose. Its
optimum temperature for activity is around 37°C.
What do you think happened to the rate of reaction when they increased the temperature
of the first test tube to 37°C?
What do you think happened to the enzyme activity when the students decreased the
temperature of the second test tube to O°C?
h) Explain what an inhibitor is and what it does.
i) The stomach produces hydrochloric acid which increases the acidity of the stomach to the
optimum pH for stomach enzymes to digest the food. However, digestive enzymes found in
the small intestine are damaged by strongly acidic conditions. How does the body avoid
damaging the digestive enzymes in the small intestine with this strongly acidic pH as the
food passes out of the stomach?
j) Give one advantage of using enzymes in industrial manufacturing processes
k.) Chemical Connections:
1. After a heart attack, the levels of certain enzymes rise in the serum. Which enzyme would you
monitor within 24 hours following a suspected heart attack?
2. Caffeine is a stimulant that is taken by many people in the form of coffee, tea, chocolate, and cola
beverages. It is also used by many athletes. Caffeine has many effects, including stimulating
lipases. Given its effect on lipases and on glycogen phosphorylase, would you predict caffeine to
be more effective as an aid to a runner in a 10K race or in a 1-mile race?
3. Caffeine is also a diuretic, which means it increases the movement of water through the kidneys
and into the urine. Why would this potentially offset its value to a distance athlete?
4. In some health food stores, it is possible to buy supplements that contain isolated enzymes. For
example, the enzyme superoxide dismutase functions as an antioxidant in cells that are exposed to
oxygen. Do you think that these supplements are likely to have significant value?