What is the role of tropomyosin in muscles?

Answer 1

Tropomyosin is the thick filament of a muscle sarcomere. It lines the span of 7 G-actin monomers along the grooves of the F-actin filament. Troponin is a trimer that consists of subunits TN-C, TN-I and TN-T. Troponin is attached to tropomyosin and its function is involved in muscle contraction.

In a powerstroke of a muscle contraction you have TN-I blocking the myosin head from attaching to the myosin binding site on the actin filament. This is the resting state. When you contract your muscles, calcium is released and attaches to TN-C. This produces a conformational change that moves TN-I away from the myosin head. In turn the myosin binds to the myosin binding site. On the myosin head there is a myosin ATPase that hydrolyzes an ATP which provides the energy for the head to bend 45 degrees. This is the powerstroke that produces muscle contraction.

Another ATP molecule will enter in and release the myosin head and calcium is pumped back into the sarcoplasmic reticulum. The resting state is restored!

Answer 2

The troponin-tropomyosin complex changes shape and sinks deeper into the groove of the thin filaments. This exposes the active sites of the actin filaments and makes them available for binding to myosin heads.

Answer 3

Short answer: Tropomyosin wraps around an actin filament to form a functional actin filament or aka. thin filament. It's purpose is involved in the powerstroke of the myosin head. It does this by kind of like a hook. If you have a hook and you grab a long rope and pull it towards you, the hook is a thick filament (myosin) and the rope is a thin filament (actin). Troppmyosin will block the hook from latching onto the rope in normal resting phase. When it is released (by calcium), you can now freely hook the rope and pull it towards you.

Long answer:

Tropomyosin wrap around actin like a slinky. It functions to block myosin from attaching to actin. This is done by troponin complex (TN-I, TN-C, TN-T). In the sliding filament model you have the thick (myosin) and thin (actin) filaments sliding past one another. This sliding action is performed by crossbridges formed between the myosin head and myosin-binding site on the actin.

Normally in resting phase, when the muscle is relaxed, the troponin complex is blocking the myosin-binding site. This prevents the myosin head from attaching to the myosin-binding site. In addition it is preventing a protein on the myosin head (myosin ATPase) from hydrolizing an ATP for what it will later use in a powerstroke. Whenever the myosin-binding site becomes available, it will always want to attach to the myosin head. This is the high affinity it has. The myosin-binding site reveals itself when calcium enters and makes a conformational change on that troponin complex (first paragraph). Actually it adheres to TN-C specifically (TN-C = troponin calcium). So when calcium attaches to troponin complex it reveals the myosin-binding site. As the myosin-binding site is revealed the head is now free to attach and the myosin ATPase is now free to hydrolyze ATP. It takes that energy to bend the myosin head 45 degrees and it attaches to the myosin-binding site. SUCCESS!

However, that's only half the story because now you need detach. Another ATP molecule comes in and it detaches the myosin head from the thin filament (specifically myosin-binding site). It's important to note here that the ATP is not hydrolyzed and it's only used to restore the resting phase. Calcium is taken back by pumps, the troponin complex rears it's ugly face and the myosin head is blocked once again.

When a person dies and no longer produces ATP, the muscles that were contracted cannot release because new ATP doesn't exist to restore the resting phase. This is rigor mortis.

Answer 4

Tropomyosin serves as a contraction inhibitor by blocking the myosin binding sites on the actin molecules.

Answer 5

The displacement of tropomyosin exposes the active sites of actin allowing cross bridge to form.