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Q2 Anskey

This document contains a quiz with multiple choice questions focused on biochemistry, specifically on amino acids, protein structure, and related concepts. It covers topics such as the structure of α-amino acids, properties of amino acids, peptide bonds, and techniques for protein analysis. The quiz aims to assess knowledge on the fundamental aspects of biochemistry.

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mrisarobles
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19 views3 pages

Q2 Anskey

This document contains a quiz with multiple choice questions focused on biochemistry, specifically on amino acids, protein structure, and related concepts. It covers topics such as the structure of α-amino acids, properties of amino acids, peptide bonds, and techniques for protein analysis. The quiz aims to assess knowledge on the fundamental aspects of biochemistry.

Uploaded by

mrisarobles
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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BIOCHEMISTRY

QUIZ # 2

Multiple Choice Questions

1. What is the basic structure of an α-amino acid?


a) A carboxyl group, amino group, hydrogen, and a hydroxyl group
b) A carboxyl group, amino group, hydrogen, and an R group
c) A carboxyl group, two amino groups, and a hydrogen
d) A hydroxyl group, amino group, and two R groups

2. Which of the following amino acids is considered non-polar?


a) Serine
b) Glutamine
c) Leucine
d) Arginine

3. The peptide bond in proteins is formed through which type of reaction?


a) Hydrolysis
b) Condensation (dehydration synthesis)
c) Oxidation
d) Reduction

4. At physiological pH (7.4), amino acids exist primarily in which form?


a) Neutral molecules
b) Zwitterions
c) Anions
d) Cations

5. Which amino acid contains a sulfur atom in its side chain?


a) Valine
b) Cysteine
c) Serine
d) Histidine

6. What is the isoelectric point (pI) of an amino acid?


a) The pH where the amino acid is fully protonated
b) The pH where the amino acid is fully deprotonated
c) The pH where the amino acid has no net charge
d) The pH at which the amino acid precipitates

7. Which amino acid is not optically active?


a) Alanine
b) Glycine
c) Proline
d) Tryptophan

8. A protein’s primary structure is determined by:


a) The sequence of amino acids
b) The hydrogen bonding between peptide chains
c) The folding of polypeptide chains
d) The interaction between R-groups

9. Which of the following amino acids has an imidazole side chain?


a) Lysine
b) Histidine
c) Arginine
d) Aspartate

10. Which force is the primary stabilizing factor in a protein’s secondary structure?
a) Hydrogen bonding
b) Covalent bonding
c) Ionic bonding
d) Van der Waals interactions
11. The α-helix and β-sheet are examples of which level of protein structure?
a) Primary
b) Secondary
c) Tertiary
d) Quaternary

12. Which amino acid has a benzyl side chain?


a) Phenylalanine
b) Threonine
c) Methionine
d) Glutamate

13. What is the primary role of chaperone proteins in cells?


a) Assisting in protein folding
b) Catalyzing peptide bond formation
c) Breaking down proteins
d) Binding to DNA

14. What happens to a protein when it is denatured?


a) Its secondary and tertiary structures are disrupted
b) Its primary sequence is altered
c) It is hydrolyzed into amino acids
d) It gains additional function

15. Which amino acid is commonly found at turns in protein structures due to its
rigid ring?
a) Alanine
b) Proline
c) Serine
d) Tyrosine

16. Which of the following amino acids is positively charged at physiological pH?
a) Lysine
b) Glutamate
c) Aspartate
d) Serine

17. Which technique is commonly used to determine the primary sequence of a


protein?
a) Edman degradation
b) X-ray crystallography
c) Nuclear Magnetic Resonance (NMR)
d) Circular dichroism

18. The bond angle in a peptide bond is rigid due to:


a) Resonance between the carbonyl and amide nitrogen
b) Hydrogen bonding
c) Van der Waals interactions
d) Electrostatic attraction

19. In protein structure, disul de bonds form between:


a) Two cysteine residues
b) Two lysine residues
c) Two proline residues
d) Two arginine residues

20. Which amino acid has the highest UV absorbance at 280 nm?
a) Tryptophan
b) Tyrosine
c) Phenylalanine
d) Alanine

21. Which amino acid has an amide functional group in its side chain?
a) Asparagine
b) Methionine
c) Serine
d) Histidine
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22. The tertiary structure of a protein is mainly stabilized by:
a) Hydrogen bonding
b) Hydrophobic interactions and disul de bonds
c) Peptide bonds
d) Electrostatic interactions

23. The quaternary structure of a protein refers to:


a) The sequence of amino acids
b) The folding of a single polypeptide chain
c) The interaction of multiple polypeptide chains
d) The hydrogen bonds in α-helices

24. A polypeptide has a net negative charge at pH 7.4. This suggests it has a high
content of:
a) Aspartate and Glutamate
b) Lysine and Arginine
c) Tryptophan and Tyrosine
d) Histidine and Proline

25. Which of the following amino acids can be phosphorylated in proteins?


a) Serine
b) Valine
c) Alanine
d) Leucine

26. Which method is commonly used to separate proteins based on size?


a) Gel ltration chromatography
b) Isoelectric focusing
c) Western blotting
d) Edman degradation

27. Which amino acid is involved in one-carbon metabolism?


a) Methionine
b) Glycine
c) Serine
d) Cysteine

28. Which structural feature makes proline unique among amino acids?
a) It has a cyclic imino group instead of a primary amino group
b) It has two carboxyl groups
c) It has a sulfur atom
d) It contains an extra hydrogen bond donor

29. Which of the following amino acids is ketogenic but not glucogenic?
a) Leucine
b) Alanine
c) Aspartate
d) Serine

30. The Bohr e ect in hemoglobin refers to:


a) The decrease in oxygen binding a nity due to increased CO₂ or decreased pH
b) The cooperative binding of oxygen
c) The transport of CO₂ by hemoglobin
d) The formation of methemoglobin
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