Question:
Study the following statements regarding contractile proteins of muscle. Identify the correct statements:
I. Actin is a protein present in thin filament present in I-band of a sarcomere.
II. Myosin forms the thick filament and contains ATPase activity in its tail region.
III. Troponin binds calcium ions and helps in exposing the active sites on thin filament.
IV. Tropomyosin actively hydrolyses ATP during muscle contraction.
Study the following statements regarding contractile proteins of muscle. Identify the correct statements:
I. Actin is a protein present in thin filament present in I-band of a sarcomere.
II. Myosin forms the thick filament and contains ATPase activity in its tail region.
III. Troponin binds calcium ions and helps in exposing the active sites on thin filament.
IV. Tropomyosin actively hydrolyses ATP during muscle contraction.
Show Hint
Actin = thin, Myosin = thick/ATPase-head.
Updated On: Jun 6, 2026
- I, II and III
- I and IV
- I and III
- I, III and IV
Show Solution
Verified By Collegedunia
The Correct Option is C
Solution and Explanation
Step 1: Concept
Muscle contraction proteins.
Step 2: Meaning
Structural and functional properties of myofibrils.
Step 3: Analysis
Actin is indeed in the thin filament/I-band (I is correct). Myosin's ATPase activity is in the head, not the tail (II is incorrect). Troponin binds calcium and moves tropomyosin to expose sites (III is correct). Tropomyosin itself does not hydrolyze ATP; myosin does (IV is incorrect).
Step 4: Conclusion
Only statements I and III are correct.
Final Answer: (C)
Muscle contraction proteins.
Step 2: Meaning
Structural and functional properties of myofibrils.
Step 3: Analysis
Actin is indeed in the thin filament/I-band (I is correct). Myosin's ATPase activity is in the head, not the tail (II is incorrect). Troponin binds calcium and moves tropomyosin to expose sites (III is correct). Tropomyosin itself does not hydrolyze ATP; myosin does (IV is incorrect).
Step 4: Conclusion
Only statements I and III are correct.
Final Answer: (C)
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