UNIVERSITY OF NEW ENGLAND

NAME:___________________________________
STUDENT NUMBER:_______________________

UNIT CODE: BCHM210

PAPER TITLE: Introductory Biochemistry and Molecular Biology

PAPER NUMBER: First and Only

DATE: Thursday 28 January 2016 TIME: 9:15 AM TO 11:30 AM

TIME ALLOWED: 2 hours and 15 minutes

NUMBER OF PAGES IN PAPER: NINE (9)

NUMBER OF QUESTIONS ON PAPER: THIRTY THREE (33)

NUMBER OF QUESTIONS TO BE ANSWERED: THIRTY THREE (33)

STATIONERY 1 6 PAGE ANSWER BOOKS 1 GENERAL PURPOSE ANSWER SHEET

PER
CANDIDATE: 0 GRAPH PAPER SHEETS 0 GEOLOGY SAMPLES

OTHER AIDS REQUIRED: NONE

CALCULATORS: PERMITTED (APPROVED MODELS ONLY)
TEXTBOOKS OR NOTES: NOT PERMITTED

INSTRUCTIONS FOR CANDIDATES:

• Candidates MAY NOT start writing until instructed to do so by the supervisor
• Please pay attention to the announcements and read all instructions carefully before
commencing the paper
• Candidates MUST write their name and student number on the top of this page and
on the General Purpose Answer Sheet
• Answer all THIRTY THREE (33) questions
• SECTION A: Answer these questions in the answer book provided
• SECTION B: Answer these questions on the General Purpose Answer Sheet
• This examination paper is worth 40% of the total marks for the unit; Section A is worth
20% and Section B is worth 20%
• You must pass this examination to pass BCHM210
• This examination paper MUST BE HANDED IN along with all supplied stationery.
Failure to do so may result in the cancellation of all marks for this examination

REMEMBER TO WRITE YOUR NAME AND STUDENT NUMBER AT THE TOP OF THIS PAGE
AND ON THE GENERAL PURPOSE ANSWER SHEET

THE UNIVERSITY CONSIDERS IMPROPER CONDUCT IN EXAMINATIONS TO BE A SERIOUS OFFENCE.

PENALTIES FOR CHEATING ARE EXCLUSION FROM THE UNIVERSITY FOR ONE YEAR AND/OR CANCELLATION
OF ANY CREDIT RECEIVED IN THE EXAMINATION FOR THAT UNIT.
 BCHM210 Trimester 3, 2015

SECTION A – PROTEINS (APPROX 1h)

This section is worth 60 marks; answer all THREE questions

QUESTION 1 (20 MARKS)

a) The figure below shows the structure of the amino acid lysine. The pK values for ionisable
groups of lysine are: pK1 (COOH) = 2.18, pK2 (NH3+) = 8.95, pKR = 10.53.
Use these values to redraw lysine showing ionisable groups in their predominant forms at pH
7 and pH 12; label each structure with the relevant pH. [5 marks]

b) Now draw lysine and a different amino acid linked via a peptide bond.
Label the peptide bond, the N-terminus and the C-terminus of your peptide. [5 Marks]
c) Name ONE example of each type of amino acid listed below: [1 mark each]
 -ve charged
 sulfur
 hydrophobic
 aromatic
 hydroxy

d) For each of the amino acids listed above, name ONE type of bond or non-bonding
interaction in which the R-GROUP participates, contributing to the stability of the native
three-dimensional structure of proteins. [1 mark each]

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 BCHM210 Trimester 3, 2015

QUESTION 2 (20 MARKS)

β-Galactosidase is an enzyme used in one of the practicals in this unit.
a) Write an equation for the reaction normally (in living organisms) catalysed by this enzyme. [2
marks]

b) Which of the six major groups of enzymes ( oxidoreductases, transferases, hydrolases, lyases,
isomerases and ligases) does β-Galactosidase belong to? Justify your answer. [2 marks]

c) What item of equipment was used to measure the activity of β-galactosidase? Explain why this
equipment is used frequently for enzyme assays. [3 marks]

d) In a class experiment to investigate the kinetics of an enzyme, the initial reaction rate (Vo)
was measured at a variety of substrate concentrations. The results are shown below.

(i) Sketch the Vo vs [S] plot for this enzyme, adding labels showing the approximate positions
on your graph for Vmax and KM. [3 marks]

(ii) Estimate the APPROXIMATE KM for the enzyme for which data is shown; explain your
reasoning briefly. [2 marks]

e) In the practical we investigated regulation of enzyme activity via regulation of

transcription, however direct regulation of enzyme activity is also important in a great many
branches of biology. Describe in detail a specific example of regulation of enzyme activity
(not enzyme production) relevant to your area of study. Use this example to explain the
importance of enzyme regulation

[8 marks]

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 BCHM210 Trimester 3, 2015

Question 3 (20 Marks)

a) The structure of proteins is described at four levels: primary, secondary, tertiary and quaternary.
Briefly explain what is referred to by each of these terms. Why are these distinctions useful? [5
marks]

b) Each level of protein structure is stabilised by chemical bonds and interactions: List the bonds
and/or effects primarily responsible for stabilising each level of structure. [5 marks]

c) The illustration below shows a molecule of haemoglobin. Describe TWO (2) aspects of
haemoglobin STRUCTURE which are important for its FUNCTION in transporting oxygen around
the body. Explain how each structural feature is required for the function of haemoglobin. [10
marks]

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 BCHM210 Trimester 3, 2015

SECTION B – Carbohydrates and Metabolism (APPROX 1h)

This section is worth 60 marks; answer all questions;
Each question is worth 2 marks

PLEASE USE THE ANSWER SHEET PROVIDED FOR THIS SECTION

Select the best answer in the multiple choice questions below:

1. Aldose sugars are
1. Very rare in biological systems
2. Characterised by a double bonded oxygen on the terminal carbon
3. Lacking in a carbonyl group
4. Characterised by a double bonded oxygen on a non-terminal carbon
2. Biological oxidation-reduction reactions always involve
1. direct participation of oxygen.
2. formation of water.
3. mitochondria.
4. transfer of electron(s).

3. If the ΔG'° of the reaction A B is 40 kJ/mol, under standard conditions the reaction:
1. is at equilibrium.
2. will not occur spontaneously.
3. will proceed at a rapid rate.
4. will proceed spontaneously from A to B

4. A furanose ring
1. Is present in fructose
2. Is a 5 membered ring
3. Is generated by high temperature oxidation of glucose
4. (a) and (b)

5. A Haworth projection of the α anomeric form of D glucose will depict

1. A straight chain structure for glucose
2. The anomeric hydroxyl group below the plane of the ring
3. The anomeric hydroxyl above the plane of the ring
4. Many hexoses linked by β 1-6 linkages

6. The following can be produced in glycolysis except

1. 2 molecules of NADH
2. 2 molecules of FADH
3. 2 molecules of pyruvate
4. 1 molecule of glucose 6 phosphate

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 BCHM210 Trimester 3, 2015

7. For each molecule of glucose converted to pyruvate in the glycolytic pathway ___
molecules of ATP are used initially (Preparatory Stage) and ____ molecules of ATP are
produced (Payoff Stage) for an overall yield of ___ molecules of ATP/glucose. The
"ATP math" is:
1. -2 + 4 = 2
2. -1 + 4 = 3
3. -2 + 5 = 3
4. -1 + 2 = 1

8. Which of the following reactions in glycolysis is the REDOX reaction?

1. Hexokinase
2. Glyceraldehyde-3-phosphate dehydrogenase
3. Pyruvate kinase
4. Phosphofructokinase-1
5. Phosphoglycerate kinase
9. What is the net yield of NADH when glucose 6-phosphate is converted to ethanol
during fermentation?
1. 0
2. 1
3. 2
4. 3
10. The net number of ATP molecules produced when one molecule of glucose passes
through the anaerobic stage of respiration is:
1. 4
2. 2
3. 3
4. 1
11. Which of the following is not a product of fermentation?
1. CO2
2. O2
3. ethanol
4. lactate

12. Which of the following statements is incorrect?

1. Aerobically, pyruvate forms the acetyl group of acetyl-CoA that enters the citric
acid cycle.
2. In anaerobic muscle, pyruvate is converted to lactate.
3. In yeast growing anaerobically, pyruvate is converted to ethanol.
4. Reduction of pyruvate to lactate regenerates a cofactor essential for glycolysis.
5. Under anaerobic conditions pyruvate does not form because glycolysis does not
occur.

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 BCHM210 Trimester 3, 2015
13. Which metabolic pathway or process is common to both aerobic and anaerobic
oxidation of sugar?
1. Citric acid cycle
2. Chemiosmosis in mitochondrion
3. glycolysis
4. oxidation of pyruvic acid to CO2

14. What substance is produced by the oxidation of pyruvate and feeds into the citric acid
cycle?
1. pyruvate
2. glucose
3. acetyl-CoA
4. O2

15. Which of the following are functions of the citric acid cycle?
1. the generation of NADH and FADH2
2. the formation of α-ketoglutarate
3. the oxidation of acetyl-CoA produced from glycolysis and fatty acid oxidation
4. all of the above

16. In a eukaryotic cell, most of the enzymes of the tricarboxylic acid cycle are located in
the
1. cytosol
2. intermembrane space.
3. inner mitochondrial membrane.
4. mitochondrial matrix

17. The glycerol phosphate shuttle functions in:

1. anaerobic glycolysis for regeneration of NAD
2. lipid catabolism
3. aerobic glycolysis to transport NADH equivalents resulting from glycolysis into
mitochondria
4. triglyceride synthesis

18. Proton pumping in the context of oxidative phosphorylation

1. is driven by the energy released from the electron flow within the inner
mitochondrial membrane
2. generates an electro-chemical gradient across the inner mitochondrial membrane
3. describes the movement of hydrogen ions across the inner mitochondrial
membrane
4. all of the above

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 BCHM210 Trimester 3, 2015
19. In aerobic cellular respiration, which generates more ATP, substrate-level
phosphorylation or oxidative-level phosphorylation?
1. substrate-level phosphorylation
2. oxidative-level phosphorylation
3. both generate the same amount of ATP
4. neither generates any ATP

20. What role does O2 play in aerobic respiration?

1. it plays no role
2. it combines with acetyl-CoA at the start of the Krebs cycle
3. it is given off as a by-product during the oxidation of pyruvate
4. it combines with H2O to help drive the formation of ATP
5. it is the final electron acceptor at the end of the electron transport chain

21. NADPH is produced during

1. glycolysis
2. the oxidation of pyruvate
3. the Krebs cycle
4. all of the above
5. none of the above

22. The pentose phosphate pathway is utilized for all of the following EXCEPT which one?
1. formation of ATP
2. generation of NADPH
3. ribose-5-phosphate synthesis
4. ribose-5-phosphate degradation
5. synthesis of pentoses

23. Energy that is released from glucose during respiration but not transferred to ATP
bonds can be detected as:
1. H2O
2. CO2
3. ADP
4. Heat

24. If one molecule of glucose is completely oxidised to H2O and CO2, a total of:
1. 38 molecules of ATP may be produced
2. 34 molecules of ATP may be produced
3. 36 molecules of ATP may be produced
4. 32 molecules of ATP may be produced

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 BCHM210 Trimester 3, 2015
25. The energetic efficiency of a car engine (petrol --> motion) is about 25%. By contrast,
the energetic efficiency of complete oxidation of one mole of glucose (glucose --> ATP)
in vivo is
1. less than 10%
2. about 15%
3. around 35%
4. more than 70%

26. Which series lists steps of the TCA in their correct order of formation:
1. Citrate, α ketoglutarate, isocitrate, succinyl CoA, succinate
2. Citrate, α ketoglutarate, cis-aconitate, isocitrate, succinyl CoA
3. Succinyl-CoA, succinate, fumerate, malate
4. Succinate, fumerate, oxaloacetate, malate,

27. The respiratory chain complex on the inner mitochondrial membrane that is flavin based,
passes electrons to Coenzyme Q and is inhibited by the rat poison rotenone is:
1. Complex 1
2. Complex 2
3. Complex 3
4. Complex 4
5. ATP synthase

28. Which metabolic pathway or process is common to both aerobic and anaerobic oxidation
of sugar?
1. citric acid cycle
2. chemiosmosis in mitochondrion
3. glycolysis
4. oxidation of pyruvic acid to CO2

29. The chemiosmotic model which links the proton motive force with ATP synthesis was
proposed by:
1. Linus Pauling
2. Melvin Calvin
3. Frederick Sanger
4. Peter Mitchell
5. Melvin Bragg
30. The “energy charge” of the cell is determined by:
1. The redox potential measured in mV
2. The extent of ionisation of the molecule
3. The quantity of energy released (kJ) if fully oxidised
4. The quantity of ATP in the cell relative to ADP and AMP

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result in the cancellation of all marks for this examination.
Writing your name and number on the front will help us confirm that your paper has been returned.