Muscle Anatomy and Troponin Complexes

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Questions and Answers

What is the length of a sarcomere in resting muscle?

  • 3.0 μm
  • 1.0 μm
  • 1.6 μm
  • 2.5 μm (correct)

Which protein binds to Ca2+ during muscle contraction?

  • Myosin
  • α-actinin
  • Tropomyosin
  • Troponin (correct)

What characterizes the A band within a sarcomere?

  • It contains thick myosin filaments. (correct)
  • It represents the area of thin filaments only.
  • It is isotropic in polarized light.
  • It is located at the Z disc.

What is the core structural feature of thin filaments in skeletal muscle?

<p>Tropomyosin and troponin complexes associated with actin. (B)</p> Signup and view all the answers

Which component of myosin is primarily involved in forming cross-bridges with actin filaments?

<p>Myosin heads (A)</p> Signup and view all the answers

What is the role of myomesin located at the M line in muscle fibers?

<p>It holds the thick filaments in place. (A)</p> Signup and view all the answers

Why do I bands stain more lightly compared to A bands in muscle tissue?

<p>I bands comprise only the portions of thin filaments that do not overlap thick filaments. (C)</p> Signup and view all the answers

Which statement about titin is correct?

<p>It provides elastic properties to thick myofilaments. (B)</p> Signup and view all the answers

What is the primary function of creatine kinase in muscle tissue?

<p>To aid in muscle fiber contraction by supplying ATP. (A)</p> Signup and view all the answers

Which protein is largest in the body and provides support to thick myofilaments?

<p>Titin (B)</p> Signup and view all the answers

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Study Notes

Organization of Muscle Fibers

  • Skeletal muscle fibers show cross-striations consisting of alternating light (I bands) and dark (A bands) bands.
  • A bands are anisotropic (birefringent under polarized light), while I bands are isotropic (do not alter polarized light).
  • Each I band is bisected by a Z disc, visible in Transmission Electron Microscopy (TEM).

Sarcomere Structure

  • The basic functional unit of muscle contraction is the sarcomere, spanning from Z disc to Z disc, measuring approximately 2.5 μm in length in resting muscle.
  • The arrangement of thick (myosin) and thin (actin) myofilaments produces the distinct A and I banding patterns.

Myosin Filaments

  • Thick myosin filaments are 1.6 μm long and 15 nm wide, located in the A band at the sarcomere's center.
  • Myosin is a complex protein (500 kDa) comprised of two heavy chains and two pairs of light chains; heavy chains form long, rod-like tails.
  • Myosin heads are globular projections that bind to actin and ATP, facilitating energy transfer during contraction.

Actin Filaments

  • Thin actin filaments are 1.0 μm long and 8 nm wide, situated between thick filaments.
  • Each G-actin monomer has a binding site for myosin and is anchored to the Z disc by α-actinin.

Regulatory Proteins

  • Thin filaments interact with two key regulatory proteins:
    • Tropomyosin: A 40-nm-long coil of two polypeptide chains that resides in the grooves of twisted actin strands.
    • Troponin: A complex with three subunits—TnT (attaches to tropomyosin), TnC (binds Ca²⁺), and Tnl (regulates actin-myosin interaction). Troponin complexes are regularly spaced along tropomyosin.

A Band and H Zone

  • A bands consist of thick filaments and overlapping thin filaments, with a central lighter zone termed the H zone, showcasing only the myosin rod portions.
  • The M line, found at the center of the H zone, comprises myosin-binding protein myomesin which stabilizes thick filaments and contains creatine kinase for ATP supply during contraction.

Protein Composition

  • Myosin and actin collectively account for over half of the total protein content in striated muscle.
  • I bands, bisected by Z discs, consist of thin filament portions that do not overlap thick filaments, causing lighter staining.
  • Titin: The largest protein in the body (3700 kDa), exhibits elastic properties and connects thick filaments to Z discs.
  • Nebulin: A large accessory protein (600-900 kDa), binds thin myofilaments laterally to help anchor them to α-actinin.

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