Explore topic-wise MCQs in Biochemistry.

This section includes 17 Mcqs, each offering curated multiple-choice questions to sharpen your Biochemistry knowledge and support exam preparation. Choose a topic below to get started.

1.

Which of the following is a false statement?

A. α-Keratin is α helical
B. Collagen is α helical
C. Hemoglobin has a quaternary structure
D. α-Keratin is β pleated structure
Answer» E.
Discussion
2.

Secondary structure is defined by _________

A. Hydrogen bonding
B. Vander Waals forces
C. Covalent bonding
D. Ionic bonding
Answer» B. Vander Waals forces
Discussion
3.

Which of the statements is false about multiple sequence alignment?

A. Both protein and nucleic acid secondary structures can be used
B. More useful in RNA
C. These alignments can be made more accurate by the inclusion of secondary structure information
D. A significant increase in accuracy
Answer» C. These alignments can be made more accurate by the inclusion of secondary structure information
Discussion
4.

A structure that has hydrogen bonds between polypeptide chains arranged side by side is?

A. Primary structure
B. α-helix
C. β-pleated sheets
D. Tertiary structure
Answer» D. Tertiary structure
Discussion
5.

A coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same chain is?

A. Primary structure
B. α-helix
C. β-pleated sheets
D. Tertiary structure
Answer» C. β-pleated sheets
Discussion
6.

β-pleated sheets are the examples of _________

A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure
Answer» C. Tertiary structure
Discussion
7.

Which of the following does not affect the stability of an α-helix?

A. Electrostatic repulsion
B. Bulkiness
C. Interaction between R groups spaced three residues apart
D. Occurrence of alanine and glycine residues
Answer» E.
Discussion
8.

SECONDARY_STRUCTURE_IS_DEFINED_BY?$

A. Hydrogen bonding
B. Vander Waals forces
C. Covalent bonding
D. Ionic bonding
Answer» B. Vander Waals forces
Discussion
9.

Which_of_the_following_is_false_statement?$

A. α-Keratin is α helical
B. Collagen is α helical
C. Hemoglobin has a quaternary structure
D. α-Keratin is β pleated structure
Answer» E.
Discussion
10.

Which of the statements is false about multiple sequence alignment?

A. Both protein and nucleic acid secondary structures can be used
B. More useful in RNA
C. These alignments can be made more accurate by the inclusion of secondary structure information
D. A significant increase in accuracy
Answer» C. These alignments can be made more accurate by the inclusion of secondary structure information
Discussion
11.

Which of the following is false about NMR spectroscopy?

A. NMR is an abbreviated form of Nuclear Magnetic Resonance
B. The intramolecular magnetic field around an atom in a molecule changes the resonance frequency giving structural information about the atom
C. The intermolecular magnetic field around an atom in a molecule changes the resonance frequency giving structural information about the atom
D. It is a technique that exploits magnetic properties of atomic nuclei
Answer» D. It is a technique that exploits magnetic properties of atomic nuclei
Discussion
12.

Which of the following are known as helix breakers?

A. Proline and glycine
B. Isoleucine and leucine
C. Valine
D. Threonine
Answer» B. Isoleucine and leucine
Discussion
13.

A structure that has hydrogen bonds between polypeptide chains arranged side by side is

A. Primary structure
B. α-helix
C. β-pleated sheets
D. Tertiary structure
Answer» D. Tertiary structure
Discussion
14.

A coiled peptide chain held in place by hydrogen bonding between peptide bonds in the same chain is

A. Primary structure
B. α-helix
C. β-pleated sheets
D. Tertiary structure
Answer» C. ‚âà√≠‚Äö√¢¬ß-pleated sheets
Discussion
15.

β-pleated sheets are the examples of$

A. Primary structure
B. Secondary structure
C. Tertiary structure
D. Quaternary structure
Answer» C. Tertiary structure
Discussion
16.

Which of the following is not true about secondary protein structure?

A. The hydrophilic/hydrophobic character of amino acid residues is important to secondary structure.
B. The ability of peptide bonds to form intramolecular hydrogen bonds is important to secondary structure.
C. The alpha helix, beta pleated sheet and beta turns are examples of protein secondary structure.
D. The steric influence of amino acid residues is important to secondary structure.
Answer» B. The ability of peptide bonds to form intramolecular hydrogen bonds is important to secondary structure.
Discussion
17.

Which of the following does not affect the stability of a α-helix?

A. Electrostatic repulsion
B. Bulkiness
C. Interaction between R groups spaced three residues apart
D. Occurrence of alanine and glycine residues
Answer» E.
Discussion