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1000 Biochemistry MCQs
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Biochemistry Questions and Answers –
Protein Secondary Structure
« Prev Next »
This set of Biochemistry Multiple Choice Questions & Answers (MCQs)
focuses on “Protein Secondary Structure”.
1. Which of the following does not a!ect 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
Related Topics
View Answer
Protein Engineering MCQ Questions
Answer: d
Biochemistry MCQ Questions
Explanation: The occurrence of Proline and Glycine residues a!ect the
Data Structure MCQ Questions
stability of an α-helix.
Bioinformatics MCQ Questions
2. Which of the following is not true about secondary protein structure? Life Sciences MCQ Questions
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
View Answer
Answer: a
Explanation: The hydrophilic/hydrophobic character of amino acid
residues is important to protein tertiary structure rather than to
secondary structure. In secondary structure, it is the steric size of the
residues that is important and residues are positioned to minimize
interactions between each other and the peptide chain.
3. β-pleated sheets are the examples of _________
a) Primary structure
b) Secondary structure
c) Tertiary structure
d) Quaternary structure
View Answer
Answer: b
Explanation: Secondary structure of proteins is of two forms α-helix and
β-pleated structures.
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4. 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
View Answer
Answer: b
Explanation: A coiled peptide chain held in place by hydrogen bonding
between peptide bonds in the same chain is α helix.
5. 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
View Answer
Answer: c
Explanation: A structure that has hydrogen bonds between polypeptide
chains arranged side by side is β-pleated sheets.
Check this: Biotechnology Books | Biochemistry Books
6. Which of the following are known as helix breakers?
a) Proline and glycine
b) Isoleucine and leucine
c) Valine
d) Threonine
View Answer
Answer: a
Explanation: Proline and glycine are known as helix breakers as they
disrupt the regularity of the alpha helical backbone conformation.
7. 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
View Answer
Answer: c
Explanation: The intramolecular magnetic field around an atom in a
molecule changes the resonance frequency giving structural information
about the atom.
8. 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
View Answer
Answer: b
Explanation: Less useful in RNA. This is because base pairing is highly
conserved than sequence.
9. Secondary structure is defined by _________
a) Hydrogen bonding
b) Vander Waals forces
c) Covalent bonding
d) Ionic bonding
View Answer
Answer: a
Explanation: Hydrogen bonding is present between the amine hydrogen
and carbonyl oxygen atoms in the peptide backbone.
10. 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
View Answer
Answer: d
Explanation: Fibrous structural protein, α-Keratin is α helical.
Sanfoundry Global Education & Learning Series – Biochemistry.
To practice all areas of Biochemistry, here is complete set of 1000+ Multiple
Choice Questions and Answers.
« Prev - Biochemistry Questions » Next - Biochemistry Questions and
and Answers – Protein Sequences Answers – Protein Tertiary and
and Evolution Quaternary Structures
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Recommended Articles:
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2. Biochemistry – Tough Questions and Answers
3. Biochemistry Questions and Answers – The Covalent Structure of
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4. Bioinformatics Questions and Answers – Protein Secondary
Structure Prediction for Globular Proteins
5. Protein Engineering Questions and Answers – Tertiary Structure of
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6. Protein Engineering Questions and Answers – Primary Structure of
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7. Protein Engineering Questions and Answers – Structure Function
Relationships – Leucine Zippers
8. Protein Engineering Questions and Answers – Structure Function
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Relationships – Integral Membrane Proteins
10. Protein Engineering Questions and Answers – Structure Function
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