This set of Biochemical Engineering Multiple Choice Questions & Answers (MCQs) focuses on “Biological Basics – Amino Acids and Proteins – Set 2”.
1. What is the function of SDS during electrophoresis?
a) Increase concentration of the protein
b) To coagulate the proteins
c) Identify the proteins
d) Denature the proteins
View Answer
Explanation: SDS is an anionic detergent. It is used to denature proteins during the process of electrophoresis or SDS-PAGE.
2. Which of these is a decapeptide?
a) Gramicidin
b) Vasopressin
c) Oxytocin
d) Aspartame
View Answer
Explanation: Gramicidin is a circular decapeptide. It has a very high significance in pharmaceutical industry.
3. Which of these amino acids contain non-polar uncharged R group?
a) Glycine
b) Lysine
c) Glutamate
d) Glutamine
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Explanation: Glycine has a non-polar aliphatic R group; Lysine has a positively charged R group; Glutamate has negatively charged R group; Glutamine has a non polar, uncharged R group.
4. Aspartate consists of positively charged R group.
a) True
b) False
View Answer
Explanation: Aspartate contains a negatively charged R group. Its net charge is negative at pH 7.0 because it consists of two carboxyl groups in it.
5. What is the function of Oxytocin?
a) Artificial sweetener
b) Contraction of smooth muscles
c) Prevent damage to RBC
d) Antibiotic
View Answer
Explanation: Oxytocin is a neuropeptide. It helps in the contraction of smooth muscles during labor.
6. What bond is formed by the dehydration of α-carboxyl group and α-amino group?
a) Glycosidic bond
b) Ester bond
c) Peptide bond
d) Hydrogen bond
View Answer
Explanation: Two amino acids are covalently bonded to each other. During this process, a water molecule ejects out to form a peptide bond, between α-carboxyl group of one species and α-amino group of the other species of amino acid.
7. Which of these amino acids does not have an aromatic R group?
a) Phenylalanine
b) Tryptophan
c) Tyrosine
d) Lysine
View Answer
Explanation: Lysine has a positively charged R group whereas all the other options have aromatic R group. This positive charged is observed at the pH 7.
8. What are the common secondary structures?
a) γ, δ
b) α, γ
c) α, β
d) β, γ
View Answer
Explanation: The common secondary structure of proteins is α and β. Their arrangements are α-helix, β-conformation and β-turns.
9. Out of these valuable protein products, which is the most varied and specified?
a) Enzymes
b) Antibiotics
c) Milk products
d) Hormones
View Answer
Explanation: Enzymes are the most varied and specialized. All the cellular reactions are catalyzed by these enzymes.
10. Which of these techniques are used for the characterization of proteins?
a) Chromatography
b) Salting out
c) Dialysis
d) Electrophoresis
View Answer
Explanation: Electrophoresis is a technique of separation of proteins based on the migration of charged proteins under the influence of an electric field. It is also a protein purification technique.
11. All 20 common amino acids are ____ amino acids.
a) α
b) β
c) γ
d) δ
View Answer
Explanation: All 20 common amino acids are α-amino acids. They have a carboxyl group and amino group bonded to the same α carbon atom.
Sanfoundry Global Education & Learning Series – Biochemical Engineering
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