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Biochem exam

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Exam study book Medical Biochemistry: Exam Preparatory manual E-Book of Sucheta P. Dandekar, Abbas Ali Mahdi - ISBN: 9788131252888 (Biochem exam)

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Biochem exam

Hydroxyproline - ANSWER: What is the name of this amino acid?

3. Polar
5. Endogenous - ANSWER: Choose the correct statements about Proline

1. Acidic
2. basic
3. Polar
4. Non-polar
5. Endogenous
6. Exogenous

3. Collagen - ANSWER: Choose a protein particularly rich in proline

1. albumin
2. haemoglobin A
3. Collagen
4. Lysosome
5. Casein

2. hydroxylation - ANSWER: What is the post-translational modicitation present in
Proline?

1. pegylation
2. hydroxylation
3. amidation
4. phosphorylation

1. Glycine, Histidine, Lysine
2. 2 peptide bonds - ANSWER: 1. Write down the names of the amino acids you see
from the N-terminus to the C-terminus
2. How many peptide bonds are in this peptide?

>8 - ANSWER: At what pH the isoelectric point of this peptide (copper peptide) could
likely be?

2 - ANSWER: How many basic residues are there in copper peptide?

2. Helix-loop-helix - ANSWER: What is the name of the motif shown in blue and red?

1. Beta hairpin

,2. Helix-loop-helix
3. Zinc finger
4. Helix-turn-helix

4. DNA binding - ANSWER: What is the main role of helix-loop-helix motif?

1. Oxygen binding
2. Protein-protein interaction
3. Zn2+ chelating
4. DNA binding
5. Catalytic activity

4. hydrogen bonds - ANSWER: What type of interaction is mostly responsible for
stabilizing antiparallel beta-sheets?

1. Van der Waals
2. hydrophobic
3. covalent bonds
4. hydrogen bonds

1. globular - ANSWER: What structure is albumin?

1. globular
2. fibrous

2. fibrous - ANSWER: What structure is keratin?

1. globular
2. fibrous

2. fibrous - ANSWER: What structure is collagen?

1. globular
2. fibrous

1. globular - ANSWER: What structure is histone?

1. globular
2. fibrous

2. fibrous - ANSWER: What structure is elastin?

1. globular
2. fibrous

Haemoglobin - ANSWER: What is the name of this protein?

, 2. it is composed of four subunits
5. porphyrin ring of heme is non-covalently associated with the alpha and the beta
subunits - ANSWER: What is the correct statements regarding haemoglobin?

1. it is composed mainly of antiparallel beta sheets
2. it is composed of four subunits
3. the oxygen is bound through the interaction with Fe3+ ions
4. it is mainly involved in the oxygen storage
5. porphyrin ring of heme is non-covalently associated with the alpha and the beta
subunits

2. patients are less likely to die of malaria - ANSWER: Choose a coorect statement
about thalassemias:

1. these are infectious diseases transmitted by mosquitos
2. patients are less likely to die of malaria
3. thalassemia major is the least severe form of the disease
4. point mutations in the myoglobin gene cause the disease

2. at pH 7.6 the aWnity of hemoglobin to O2 is the highest
3. the highest change in the O2 saturation is between 20-40 mm Hg - ANSWER: How
does the pH affect the oxygen binding affinity of haemoblobin? Choose the correct
statements:
1. at pH 7.2 the aWnity of hemoglobin to O2 is the highest
2. at pH 7.6 the aWnity of hemoglobin to O2 is the highest
3. the highest change in the O2 saturation is between 20-40 mm Hg
4. the highest change in the O2 saturation is between 80-100 mm Hg

Hydrolases - ANSWER: Name the general group of enzymes mediating the reaction
below:

2. this is an example of competitive inhibition
3. if the curve #2 represents an uninhibited reaction then the curve #3 represents the
inhibited reaction
5. Vmax in the presence of inhibitor can be achieved by increasing the amount of
substrate - ANSWER: Based on the presented Lineweaver-Burk plot, choose the
correct statements:
1. this is an example of uncompetitive inhibition
2. this is an example of competitive inhibition
3. if the curve #2 represents an uninhibited reaction then the curve #3 represents the
inhibited reaction
4. if the curve #2 represents an uninhibited reaction then the curve #1 represents the
inhibited reaction
5. Vmax in the presence of inhibitor can be achieved by increasing the amount of
substrate

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