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Supplementary Exercises - Final Exam: Lesson 7 - Nucleotides

The document consists of supplementary exercises for a final exam covering topics such as nucleotides, enzymes, carbohydrates metabolism, and the oral cavity. It includes questions about molecular structures, enzyme functions, metabolic pathways, and clinical cases. Each section requires students to define terms, analyze diagrams, and explain biological processes.

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ken philips
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100% found this document useful (1 vote)
16 views13 pages

Supplementary Exercises - Final Exam: Lesson 7 - Nucleotides

The document consists of supplementary exercises for a final exam covering topics such as nucleotides, enzymes, carbohydrates metabolism, and the oral cavity. It includes questions about molecular structures, enzyme functions, metabolic pathways, and clinical cases. Each section requires students to define terms, analyze diagrams, and explain biological processes.

Uploaded by

ken philips
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd
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SUPPLEMENTARY EXERCISES – FINAL EXAM

LESSON 7 – NUCLEOTIDES

1. Regarding the figure below:

3
1

a) What is the name of the molecule?


b) Identify its main components:

1:

2:

3:

c) Which part of the molecule carries the genetic information?

d) In which kind of secondary structure is this molecule typically found?

e) Which molecule is its precursor? Name it and draw a schematic representation.


2. Regarding the figure on the right:
a) Indicate the 3’ end and the 5’ end

b) Write its complementary sequence, indicating its


directionality.

c) What kind of secondary structure does this molecule form?

d) Give three examples of different types of this molecule,


indicating their function:
1. Type:
Function:

2. Type:
Function:

3. Type:
Function:

3. Explain the main differences in between eukaryotic and prokaryotic mRNA:


4. Identify the compounds and/or bonds in the figure:

A)

B)
C)

D)

F)
E)

a) _______________________
b) _______________________
c) _______________________
d) _______________________
e) _______________________
f) _______________________
5. Draw a schematic representation of the central dogma of molecular biology
LESSON 8 – ENZYMES

1. Define the following terms related to enzymes:


a) Biocatalyst

b) Active site

c) Cofactor

d) Km (Michaelis constant)

2. Examine the following diagram

a) Indicate which colour represents the reaction in the presence of the enzyme

b) Explain how the enzyme speeds up the reaction

c) What happens to the total free energy (ΔG) of the reaction when an enzyme is
added? In the plot, which letter represents ΔG?

d) What does B represent? What is produced after applying B?


3. Imagine you just have discovered a new enzyme and you are characterizing it in
the lab. After the first day of experiments, you get the following data:

[S] (mM) Vo (μmol/min)


24 11.18
56 21.50
112 28.34
192 34.41
280 38.05
392 41.60
403 42.12
458 42.91
871 42.97

a) Indicate the Km:


b) What would be the velocity if the substrate concentration is set to 150 mM? (you
need to use the Michaelis-Menten equation and a calculator).

4. The following graph represents the same reaction in the presence and in the
absence of an inhibitor

a) Which reaction is taking place in the absence of the inhibitor?

b) What type of inhibition is taking place here?

c) What is the Km in the presence of the inhibitor (Kmi)? And the Vmax?

d) How can this type of inhibition be overcomed?


5. The following graph also represents a reaction in the presence and in the
absence of an inhibitor.

a) Which reaction is taking place in the absence of the inhibitor?

b) What type of inhibition is taking place here?

c) Indicate the Km, Km inhb, Vmax and Vmax inhb

d) Which plot represents the reaction where the enzyme has the highest affinity for
the substrate?

6. Classify the following cases of inhibition as competitive, non-competitive, or


irreversible:
a) Cyanide binding to Fe2+ in the electron transport chain:
b) A drug that is very similar to the natural substrate of an enzyme, and binds to the
active site:
c) A toxin that covalently binds to an enzyme modifying its active site:
d) A drug that binds with a weak interaction to the allosteric site:
7. Case study
A 45-year-old male patient visits the clinic complaining of persistent joint pain and
swelling in his knees, which worsens with physical activity. Upon examination, the
doctor diagnoses osteoarthritis, an inflammatory condition. The patient is prescribed
ibuprofen, a non-steroidal anti-inflammatory drug (NSAID), for pain relief.
1. Explain the role of prostaglandins in the inflammation observed in this patient’s
condition.

2. Ibuprofen is a non-selective COX inhibitor. How does Ibuprofen affect the


synthesis of prostaglandins, and what are the potential side effects related to
COX-1 inhibition?

3. Describe the difference between COX-1 and COX-2 in terms of their functions
and expression

4. If the patient were to use a selective COX inhibitor instead, how would this
influence prostaglandin production and the risk of side effects? Provide
examples of selective COX inhibitors.
LESSON 10 – CARBOHYDRATES METABOLISM
1. Indicate whether the following statements are true or false, justifying your
answer:
a) Glycolysis occurs in the cytoplasm and produces two net ATP molecules per
glucose.

b) Glycogenolysis is the formation of glycogen from glucose.

c) The Krebs cycle takes place in the cytoplasm.

d) Lactic fermentation occurs when there is a lack of oxygen.

e) Gluconeogenesis can use lactate, glycerol, and amino acids as precursors.

f) The electron transport chain generates a proton gradient in the mitochondrial


matrix.

g) Hepatic glycogen is the main energy source during intense and prolonged
exercise.

2. Fill in the blanks


a) ________ is the metabolic pathway responsible for replenishing NAD+ in the
absence of oxygen.
b) ________ and ________ require glucose as their sole energy source. As well as
__________ when there is low availability of oxygen.
c) During the Krebs cycle, ________ is released, and the coenzymes ________ and
________ are reduced.
d) ________ is the process through which glucose is stored as glycogen.
e) Hexokinase converts glucose into ________ during the first step of glycolysis.
3. Match each process with its cellular location:
a) Glycolysis à ______________
b) Krebs cycle à ______________
c) Electron transport chain à ______________
d) Gluconeogenesis à ______________
e) Glycogenesis à ______________

4. Answer the questions regarding the diagram below:

A B C

I. Does A require oxygen?

II. Indicate the energy output of A in terms of ATP and NADH

III. How many rounds of B will be carried out from a glucose molecule?

IV. In a scenario with high ATP and low ADP concentrations, will B be
activated or inhibited? At which point/s will this regulation occur?
V. What about in A? Describe the regulation in a high-ATP/low ATP
scenario.

VI. Indicate in which metabolic routes is insulin involved and briefly


describe its activity.

VII. Where does C occur?

VIII. Which molecule acts as the last electron acceptor in C and what is the
end-product of that reaction?

5. Make a schematic representation of the Cori Cycle


6. Clinical Case
A patient arrives at the clinic with severe hypoglycemia. After tests, a deficiency in the
enzyme glucose-6-phosphatase is identified. Answer:
a) Which metabolic process is affected?

b) What are the most likely metabolic consequences?


LESSON 11 – THE ORAL CAVITY

1. List 3 important functions of saliva:

a) ________________

b) ________________

c) ________________

2. What can be an origin of the acidification of the oral cavity?

3. Define biomarker and list 3 examples

4. What role does saliva play in the formation of bacterial plaque?

5. What effect does acidification of the oral cavity have on the colonization of
Streptococcus mutans?

6. Describes the main functions of metalloproteinases in the extracellular


matrix

7. What factors can cause an imbalance in metalloproteinase levels in the oral


cavity?

8. What consequences can this imbalance have?

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