Unit 2 Module 1 continued

2.1.15 Nucleotides coding molecules

Nucleic acids in living
organisms

Nucleotides are monomers of

nucleic acids

What does DNA stand for?

Where is DNA found in a human cell?
Which three components make up a
nucleotide?
What type of reaction links these
together?
List the five nitrogenous bases found in
nucleotides.

Nucleotides common
features
Draw and label a simple diagram of a
nucleotide.

From nucleotides to nucleic

acids

Which parts of two consecutive

nucleotides attach to each other?
What forms the backbone of a nucleic
acid?
Which groups will be left over at either
end of the polymer?
What is the identity of the sugar
molecule in DNA and RNA?

Organic bases are either

Which bases are purines and which are

Joining nucleotides together

DNA:
Adenine:

RNA:
Cytosine:

Uracil:

purines or pyrimidines

pyrimidines?

Thymine:

Guanine:

2.1.16 DNA information storage

How many polynucleotide strands create one DNA molecule?
DNA is a stable
polynucleotide

What holds these polynucleotides together?

Why is it important that DNA is a stable molecule?
What does antiparallel mean?

Hydrogen bonding
and base pairing
getting it right

What are the base pairing couplets in DNA?

Each polymer strand does not lie flat, but coils up into what
shape?
The two chains twist around each other, giving what final
shape to a DNA molecule?
1)
Describe the sequence of events which occur when a DNA
molecule is replicated.

2)
3)
4)

Making copies
Francis Crick, codiscoverer of DNA

Why is DNA replication described as semi-conservative?

Which part of the DNA molecule contains the genetic code?
Fill in the sequence of bases which would be found on this
DNA strands complementary strand.
If the top strands sugar-phosphate backbone runs from left
to right, which way does the other ones run?
If 17% of a DNA molecules bases are thymine, what
percentage are cytosine?

T-T-C-C-G-A-C-A-G-T

2.1.17 Reading the instructions

RNA is different

Give two ways in which the structure

of RNA monomers differs from the
structure of DNA monomers.
How is the structure of the final RNA
molecule different to a DNA molecule?
What are the base pairing couplets in
RNA?

The base-pairing rules apply

Which base never appears in RNA?

Give the sequence of RNA bases that is
complementary to this DNA strand.

Three forms of RNA

DNA: A-T-T-A-G-A-C-C-G-T-G
RNA:

What are the three types of RNA?

What do the sequences of bases on
DNA code for?
What does the term gene mean?
mRNA:
Explain the functions of the three types
of RNA in protein synthesis.

What are the instructions for?

rRNA:
tRNA:

Place the following statements in the

order which correctly describes the
sequence of events which leads to
protein synthesis.

1. An mRNA strand is formed through base pairing.

2. tRNA leaves the ribosome.
3. mRNA attaches to a ribosome.
4. The amino acid joins the growing polypeptide chain.
5. The gene for a particular protein is exposed.
6. The DNA double helix is unzipped.
7. The ribosome moves along the mRNA strand.
8. tRNA holding an amino acid attaches to the ribosome.
9. The new strand leaves the nucleus.

Quick quiz
True or false?
1)
2)
3)

Uracil is a purine.
Cytosine is complementary to guanine.
The two strands of a DNA molecule are identical.

4)
5)
6)

Purines break down into uric acid, which causes gout.

Nucleic acid bases always contain nitrogen.
Ribose is a six carbon sugar.

2.1.18 Enzymes are globular proteins

All enzymes are proteins

Substrate:

A short recap: define the following terms.

Globular
Hydrophilic:
Secondary

Why are enzymes described as specific?

Glyoxalase 1

The active site is a tiny part

of an enzyme

What feature of an enzyme allows it to bind to its

substrate?
What is the job of most amino acids in an enzyme?
What is an enzymes active site?
What is a catalyst?

Catalysts in nature
Why are enzymes often used as industrial catalysts?
Substrate and product

Write down a word equation for the reaction catalysed by

lactase.

2.1.19 Inside and out where enzymes work best

Organisms vary considerably
Enzymes and endotherms

What types of conditions might change

the shape of a protein?
Why is regulating body temperature
worthwhile for birds and mammals?
What is a heterotroph?

Nutrition and digestion

enzyme locations

Enzymes and protection

What is the difference between

intracellular and extracellular
enzymes?
Even autotrophs (organisms which
dont need to digest) contain enzymes.
Why might this be?
Why do white blood cells contain
enzymes which can break down
substances?
What are white blood cells digestive
enzymes contained in?

2.1.20 Enzyme action

Draw a diagram showing the activation energy

for a reaction.
Falling apart and staying
together
What is the reason for boiling non-reducing
sugars in acid, when testing for their presence?
How do enzymes increase the rate of a reaction?
From one stable molecule to
another

Why do cells need enzymes in order to live?

Why is enzyme action compared to a lock and
key?

Not just shape more about fit

Holding it all together the

induced fit hypothesis

What happens after the key has entered the

lock?
How is the substrate held in place within the
active site?
What name is given to the enzyme while its
substrate is bound?
Why do the products leave the active site?

Carbonic anhydrase, an enzyme in

blood

What is the name for this theory of enzyme

action?
A carbonic anhydrase molecule takes about one
s (microsecond) to catalyse its reaction. How
many reactions would be catalysed per minute
by 1000 enzyme molecules?

2.1.21 Enzymes and temperature

When a substance is heated, what
happens to the kinetic energy of its
molecules?
Heat and kinetic energy

What two effects does this have on

collisions between molecules?
So what effect does heat have on
enzyme activity?
Why can heat break bonds within an
enzyme?

Heat, vibration, breaking

bonds and denaturation

What happens if an enzymes bonds

begin to break?
Why does this impair the enzymes
activity?
What is the name of this process?
What is the meaning of the term
optimum temperature?

Speeding up and slowing down

optimum temperature

In what type of habitat might an

organism need enzymes with
particularly high optimum
temperatures?
How might those enzymes differ from
normal ones to cope with the
temperature?
On the reverse of this sheet, plot a graph using the data on the next page, and determine what the optimum temperature of this
enzyme is:

Temperature / C

Rate of reaction / mol product

formed per minute

10

20

19

30

40

40

58

50

31

60

2.1.22 Enzymes at work pH effects

What does pH measure?
What is pH?
What pH range is acidic?
What are hydrogen ions attracted to?
pH and bonds

pH and active sites

Optimum pH varies between
enzymes
pH and location

How can hydrogen ions alter the shape

of an enzyme?
How will hydrogen ions interfere with
substrate binding to the active site?
Why does a change from the optimum
pH affect the rate of a reaction?
What is the optimum pH for the
enzyme pepsin?

A UV spectrometer can be used to measure the rate of a

reaction. The products of some reactions absorb UV light
by recording how quickly this absorbance changes, the
spectrometer can calculate how quickly the concentration
of the product is changing. This produces data like that in
the table to the left.

2.1.23 Enzymes at work concentration effects

Increasing the substrate
concentration

In figure 1, why does increasing the

substrate concentration above a
certain level no longer increase the
rate of reaction?
Why is it important to only record the
initial rate of reaction?

Increasing the enzyme

concentration

Describe the sequence of events which

occurs when enzyme concentration is
increased for a fixed concentration of
substrate.

Initial reaction rate

Limiting factors
Enzyme and substrate
concentrations in cells

What happens to the reaction rate as

the reaction proceeds?
When should the reaction rate be
measured in order to give fair results?
Define the term limiting factor.
Why can enzymes be kept at much
lower concentrations than substrates?
How might a cell reduce an enzymes
activity?

1)
2)
3)

2.1.24 Enzymes at work inhibitors of action

Inhibitors of enzymecontrolled reactions
Competitive inhibitors

What is an enzyme inhibitor?

How do competitive inhibitors work?
How can competitive inhibition be
overcome?

Ampicillin is a competitive inhibitor

of bacterial enzymes

Non-competitive inhibitors

How does this work?

How do non-competitive inhibitors
differ from competitive ones?
How do non-competitive inhibitors
reduce enzyme activity?
What effect will increasing the
substrate concentration have on the
rate of reaction?
How might you test whether an
inhibitor is competitive or noncompetitive?

Permanent inhibitors

Why might non-competitive inhibitors

be deliberately produced by the cell?
How do permanent inhibitors differ
from reversible inhibitors?

2.1.25 Enzymes at work coenzymes and prosthetic groups

What is a cofactor?
Enzymes shaping up
What three types of cofactor exist?
Where do coenzymes bind to their
enzyme?
How are coenzymes similar to
substrates?
How are coenzymes similar to
enzymes?
Why is vitamin B3 essential for human
health?

Coenzymes
The iron-containing haem group is a
vital part of haemoglobin

What is a prosthetic group?

What can prosthetic groups
contribute to a protein?
Which metal ion is vital to the
function of carbonic anhydrase?
What is the purpose of the reaction
catalysed by carbonic anhydrase?
How can inorganic ions affect reaction
rates?
What two features of an enzyme can
inorganic ions affect?
Which halide ion is vital to the
function of amylase?

2.1.26 Interfering with enzymes poisons and drugs

Why is potassium cyanide deadly?
Deadly poisons

Replacement enzymes and

cystic fibrosis
Ethylene glycol poisoning

Would increasing the concentration of

oxygen a patient breathed save them from
cyanide poisoning? Explain your answer.
Why are enzyme tablets prescribed to cystic
fibrosis sufferers?
Why must these tablets resist acid?
Where is ethylene glycol found?
Why is it dangerous?

Ethanol and ethylene glycol.

Competitive inhibitors often have
similar shapes to the substrates
they inhibit.

What is given as a treatment for ethylene

glycol poisoning?
How does this help?
1)

Snake venom an enzyme and

toxin cocktail

List four components of snake venom and

explain how they help the snake kill its
prey.

2)
3)
4)

Quick Quiz
True or False?
1.
2.
3.
4.
5.
6.
7.
8.

Enzymes increase reaction rate by increasing the stability of the products.

Competitive inhibitors have a similar shape to an enzymes substrate.
Higher hydrogen ion concentration gives higher pH readings.
Increasing enzyme concentration increases reaction rate.
The pH of the human stomach is around 2.
Prosthetic groups are polypeptides.
Carbonic anhydrase converts CO2 to carbonic acid.
Heat is a measure of the kinetic energy of a substances molecules.

2.1.27 Investigating enzyme action 1

What can we investigate?

Dependent and independent

variables

How can you measure the rate of an

enzyme-catalysed reaction?
What is the difference between
dependent and independent variables?
If you record the rate of a reaction at
different pH levels, which variable is
dependent?
What can you do to the independent
variable to increase the accuracy of
your results?
In an enzyme-catalysed reaction, which
variables are particularly important to
control?

What needs to be controlled?

What is the best way to regulate

temperature?
Why is using enzyme in living tissue
less accurate than using purified
enzyme?
How can pH be regulated?

Timescales, rate and control

tests

Why might using high enzyme

concentrations make getting accurate
results difficult?
What is the relationship between time
and reaction rate?
Which variable always goes on the yaxis of a graph?
What is the purpose of a control test?

2.1.28 Investigating enzyme action 2

Why is it best to record the initial rate
of reaction?
How can you do this?

Following an enzymecontrolled reaction

Sketch a graph and label it to show

how you would measure the initial rate
of a reaction.

How do you calculate the gradient of a

tangent?

Examples of enzyme
investigations

Write a method for an investigation

into the effect of pH on amylase
activity.

2.1.29 Enzymes and metabolism an overview

Catalytic power

Control of metabolic
sequences

Why is it vital to control the power of

enzymes?

Explain how end-product inhibition

works.

Why is ATP synthase vital for life?

Some enzymes are crucial to
life
Write a word equation for the
conversion of ADP to ATP.
What is the cause of problems with the
bodys proteins?
Which protein does not work correctly
in sufferers of phenylketonuria (PKU)?
Inborn errors of metabolism

If undiagnosed, what does this

condition lead to?
Phenylalanine is an essential amino
acid. How might this affect the way
PKU sufferers are treated?