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A2.
a
Figure 12.8
A fat found in a vegetable oil.
a
b
c
A3.
a
b
c
The fat is saturated because the alkyl groups in the molecules (CH3(CH2)14)
contain only single carboncarbon bonds. Alkyl groups with the general formula
CnH2n + 1 are saturated.
i HOCH2CHOHCH2OH and CH3(CH2)14COOH
ii water
iii hydrolysis
Q4.
Describe the types of fatty acids that combine with glycerol to form:
a saturated fats
b mono-unsaturated fats
c polyunsaturated fats
A4.
a
b
c
The glucose molecule has five polar OH groups which form hydrogen bonds with
water. As a result glucose is highly soluble in water.
Q7.
Glucose is described as a monosaccharide, maltose as a disaccharide and glycogen as
a polysaccharide.
a What is the difference between these three types of carbohydrate?
b What type of reaction is involved in converting glucose to maltose and then to
glycogen?
c Which functional group in the molecules is involved in these reactions?
A7.
a
b
c
Figure 12.21
The structure of lactose.
a
b
c
d
A8.
a
b
Our digestive system secretes enzymes that can rapidly hydrolyse lactose to
glucose, which is used in respiration. We do not produce enzymes that can break
down cellulose, the main carbohydrate in celery.
i
ii
i
ii
A9.
a i, ii
b i, ii
Q10.
Starch, glycogen and cellulose are all polymers that contain glucose monomers.
Explain why the human body can completely digest the starch and glycogen but
cannot digest cellulose to any great extent.
A10.
Humans lack the enzyme (cellulase) that catalyses the hydrolysis of cellulose to form
glucose.
Q11.
Write a chemical equation for:
a the hydrolysis of sucrose
b the hydrolysis of tristearin (see Figure 12.3)
A11.
a
E2.
Why must vegetarians ensure that their diet contains complementary proteins?
AE2.
The human body only manufactures some of the required amino acids. The other
amino acids, called essential amino acids are provided in our food. Animal protein
provides all these essential amino acids. Vegetable protein is often deficient in one or
more essential amino acids.
E3.
A healthy diet includes proteins that include essential amino acids. Why should
essential amino acids be included in a healthy diet?
AE3.
Nine out the 20 amino acids required by the body cannot be manufactured in the
body. They must be provided by the food we eat. These are called essential amino
acids.
E4.
Kwashiorkor or proteinenergy malnutrition is a disease found in some traditional
African societies. Find out more about this disease and its causes.
AE4.
Lack of protein in the diet of young children causes a form of starvation known as
proteinenergy malnutrition. It is the most common form of death of young children
in the developing world.
Q12.
What two functional groups are present in all amino acids?
A12.
amino and carboxyl
Q13.
Draw the structural formula of glycine as it is likely to exist in:
a an acidic solution
b an alkaline solution
c neutral solution.
Q14.
With the aid of Table 12.7 on page 189 of the student book:
a draw structural formulas of serine and cysteine
b write an equation to show the formation of a dipeptide from these amino acids
c name the type of reaction in part b.
A14.
a
b
c
H2NCH(CH2OH)COOH + H2NCH(CH2SH)COOH
H2NCH(CH2OH)CONHCH(CH2SH)COOH + H2O
condensation
The folding of a section due to, for example, hydrogen bonding between peptide links
is known as the secondary protein structure.
Figure 12.31
A17.
Q18.
Use the information in Table 12.7 on page 189 of the student book to sketch the
structural formula of the tripeptide that would be represented as ala-ser-val.
A18.
Q19.
a
b
c
Find the names and describe the functions of two enzymes in the body.
Explain why the action of enzymes justifies the statement Enzymes make life
possible.
Why is the action of an enzyme often described as operating like a lock and
key?
Enzymes in the body include pepsin, which hydrolyses peptide bonds of certain
amino aids:
DNA polymerase which replicates and repairs DNA
lactase which breaks down the sugar lactose in the small intestine
salivary amylase which breaks down polysaccharides in the mouth.
Almost all the chemical reactions occurring in living creatures are controlled by
enzymes. Enzymes speed up the reactions that are essential for life processes by
as much as 1010 times; reactions that do not contribute to the functioning of a
creature are not catalysed and occur at much slower rates.
The shape and functional groups in the active site of the enzyme allow it to bind
only with certain substrates so that only a specific reaction is catalysed. In a
similar way, a lock will only open using a key of a certain shape.
Q20.
What are the main differences between enzymes and inorganic catalysts?
A20.
Compared to inorganic catalysts, enzymes can produce much faster reaction rates,
operate under milder conditions and are highly selective. Whereas an inorganic
catalyst might increase the rates of many different reactions, enzymes are usually
effective for just one reaction.
Q21.
The enzyme carbonic anhydrase catalyses the decomposition of carbonic acid
molecules to carbon dioxide and water in the lungs. When heated to more than 60C,
the enzyme becomes denatured.
a What is meant by the term denatured?
b Describe the events that usually occur to the structure of an enzyme when it is
denatured.
c Does the primary structure of the carbonic anhydrase enzyme change during this
process?
d Why is the functioning of the enzyme closely related to its tertiary structure?
A21.
a
b
c
d
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Q24.
Explain why doctors sometimes rely on information from a number of tests and
observations to make a diagnosis rather than relying solely on the presence of a
protein marker.
A24.
A number of factors other than the disease under investigation may lead to an increase
in the level of a specific protein marker.
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Q26.
By referring to Figure 12.3, write reactions that show:
a the hydrolysis of the fat tristearin
b the complete oxidation of the products from part a
A26.
a
Q27.
The structure of a fatty acid, linoleic acid, is shown in Figure 12.39.
a Name the chemical needed to convert linoleic acid into a lipid.
b Draw the structure of the lipid made from linoleic acid.
c Name and circle the functional group found in the lipid molecule.
d Classify the lipid as saturated, mono-unsaturated or polyunsaturated.
e Is this fat likely to be a solid or liquid at room temperature? Explain.
Figure 12.39
The structure of linoleic acid.
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glycerol
c
d
e
Q28.
a
b
A28.
a
i, ii
enzyme
Q29.
Why is glycogen sometimes called animal starch?
A29.
Glycogen is the main storage polysaccharide in animals. It therefore fulfils the same
role in animals that starch does in plants.
13
H2NCHCH3CONHCH2COOH
H2NCH2CONHCHCH3COOH
6 (using each amino acid once in each peptide)
very large numbers
Q33.
Aspartic acid is one of the non-essential amino acids (Figure 12.40). It exists as a
zwitterion at pH 2.8.
Figure 12.40
The structure of aspartic acid.
a
b
Name:
i the acidic functional group
ii the basic functional group.
Draw the structure of the molecule as it is most likely to exist in a solution at:
i pH much more than 2.8
14
i
ii
carboxyl
amino
Circle the peptide linkages in the part of the protein chain shown in Figure 12.41.
Write the formulas of the amino acids that made up this part of the chain.
Where in the body does hydrolysis of proteins to form amino acids take place?
Figure 12.41
A section of a protein molecule.
A34.
a
b
c
H2NCHCH3COOH; H2NCH(CH2SH)COOH
H2NCH2COOH
H2NCH(CH2OH)COOH
stomach and small intestine
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(i.e. NH2 and COOH are not joined to the same carbon)
Q37.
Scientists have spent many years trying to develop a form of the protein insulin that
can be given to diabetics orally rather than by injection. Suggest an aspect of the
chemistry of proteins that has so far prevented insulin from being taken orally.
A37.
Proteins are readily denatured by acids. Stomach acid has prevented the ingestion of
the protein insulin. The protein is hydrolysed into its component amino acids during
digestion.
Q38.
Proteins are often described in terms of their primary, secondary and tertiary
structures. What is the difference between these levels of structure and how does each
contribute to the role of the protein?
A38.
Primary structure: the sequence of the amino acids that make up the polymer chain.
This determines the entire shape of the protein.
Secondary structure: the coiling, folding or pleating of the protein chain caused by
hydrogen-bonding interactions of adjacent amino acids. These regular structures
extend along one dimension like coils in a spring and are important in fibres such as
hair and wool.
Tertiary structure: the bending and folding of the protein chain to form a compact
three-dimensional shape. These globular shapes with a low surface to volume ratio are
important for proteins in solution such as enzymes in blood.
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17
The steps in the action of an enzyme involve, in particular, an active site and a
substrate. With the use of a diagram describe in detail the action of an enzyme.
The forces of attraction that enable a substrate to bind to an active site can vary.
Describe four such forces.
A43.
a
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A44.
a
b
c
Enzymes are much faster, operate under milder conditions and are more selective
than inorganic catalysts.
Tests could include a study of the effect of the enzyme on human health and on
the environment.
Issues to consider when answering this question include the potential hazards
associated with the development of new organisms and enzymes.
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Q46.
a
b
c
A46.
a
b
c
Condensation reactions involve the linking together of two small molecules and
the elimination of a small molecule, usually water. Hydrolysis reactions consume
water and they can often be regarded as the reverse of condensation reactions.
Vital biochemical processes include condensation reactions (e.g. synthesis of
lipids, proteins and polysaccharides) and hydrolysis reactions (e.g. digestion).
i
ii
iii
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a
b
c
d
By referring to Figure 12.33 on page 195, draw the structure of the dipeptide
produced when the ACE enzyme catalyses the conversion of angiotensin I to its
active form.
Identify the amino acids formed when the amide functional group is hydrolysed.
List the types of bonds involved at the active site of ACE when it is catalysing
this reaction.
The other molecule produced is known to stimulate the constriction of blood
vessels which can lead to an increase in blood pressure. It is a small polypeptide
called angiotensin II that contains the amino acid sequence asp-arg-val-tyr-ilehis-pro-phe. What is the number of each of the following types of functional
groups in angiotensin II?
i amide (peptide)
ii carboxyl
A47.
a
b
c
d
histidine, leucine
iondipole interaction, hydrogen bonds, ionic interactions
i 7 amide
ii 1 terminal carboxyl group, 1 carboxyl group on the Z group of asp
Q48.
A fatty acid that was extracted from sunflower oil is analysed in a laboratory in a
number of ways.
a Using IR spectroscopy, it was deduced that the fatty acid is unsaturated. Explain
what feature of the IR spectrum would lead to such a conclusion.
b The unsaturated fatty acid was reacted quantitatively with hydrogen gas to
determine the number of double bonds per molecule. A 0.0102 mol sample of the
fatty acid reacted with exactly 500 mL of hydrogen gas, under SLC conditions,
for the complete conversion of the fatty acid sample to a saturated fatty acid.
i What type of reaction occurred between the unsaturated fatty acid and
hydrogen gas?
ii Calculate the amount, in moles, of hydrogen gas that reacted with the fatty
acid.
c Determine the number of double bonds per molecule.
d Use the data in Table 12.1 to identify the unsaturated fatty acid.
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n=
1 mol of fatty acid reacts with 2 mol H2. Acid contains 2 double bonds.
For example, linoleic acid
Q49.
From many thousand proteins in a human tissue sample, a research scientist needed to
separate and identify individual proteins that might be used as markers for particular
diseases. Briefly describe how each of these analytical techniques could be used in
such a process.
a HPLC
b proton NMR spectroscopy
c IR spectroscopy
d mass spectroscopy
A49.
a
b
c
d
HPLCseparation of proteins
proton NMR spectroscopystructure
IR spectroscopyfunctional groups
mass spectroscopymolar mass
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