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Q: Which myofilament has a binding site for myosin head?
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What protein shields the myosin-binding site preventing contraction from happening at rest?

ATP entering myosin head


What is the role of tropomyosin in muscles?

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!


What is the role is tropomyosin muscle?

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.


What molecule has a binding site for myosin heads?

Myosin heads bind to the actin binding site, and also has a part where ATP binds


What has the author Daniel L Kennedy written?

Daniel L. Kennedy has written: 'Photoaffinity labeling of the ATP binding site of skeletal myosin' -- subject(s): Myosin


What affect does calcium have on troponin and tropomyosin?

Calcium produces a conformational change on the troponin subunit TN-C to allow the myosin head to attach to the mysoin binding site on the actin filament. Without calcium there muscle contraction cannot begin.


Active sites on the actin become available for binding when?

C: Calcium binds to troponin. The troponin is a filament in the actin strand, and the active site needs to be uncovered so that the myosin head can bond and therefore pull the muscle to contract it.


What role does ATP play in muscle contraction?

The role ATP plays in muscle contraction is that ATP binds to sites on myosin heads, inducing a conformational change in the actin binding site and reducing the affinity for the actin substrate. Hydrolysis of ATP then cocks the myosin head and moves it closer to the z disk. Release of ADP increases the affinity of the actin binding site and a power stroke moves the head roughly 100 angstroms closer to the z disk. In short, after the power stroke, ATP is hydrolyzed to release the myosin heads from actin so that they can go to the next binding site on the actin filament. It's sort of like reloading the myosin gun.


Why is calcium needed for muscle contraction?

Yes, calcium is necessary for the release of neurotransmitters that cause a muscle to initiate a contraction. Calcium is also needed to bind to the troponin-tropomyosin complex causing it to change position so the myosin head can attach to the actin molecule which results in contraction.


What chemical ion is responsible for initiating the contraction of a muscle fiber?

Calcium ions bind to the thin filament ( actin ), turn it and expose the binding site to the thick filament (myosin ).


What blocks a bonding site in muscle?

Several things do. Neuromuscular-blocking drugs block neuromuscular transmission at the neuromuscular junction causing paralysis. Quaternary ammonium muscle relaxants are quaternary ammonium salts used as drugs for muscle relaxation, most commonly in anesthesia.When a muscle is in a resting state, actin and myosin are separated. To keep actin from binding to the active site on myosin, regulatory proteins block the molecular binding sites. Tropomyosin blocks myosin binding sites on actin molecules, preventing cross-bridge formation, which prevents contraction in a muscle without nervous input.Several things do. Neuromuscular-blocking drugs block neuromuscular transmission at the neuromuscular junction causing paralysis.Quaternary ammonium muscle relaxants are quaternary ammonium salts used as drugs for muscle relaxation, most commonly in anesthesia.Tropomyosin blocks myosin binding sites on actin molecules, preventing cross-bridge formation, which prevents contraction in a muscle without nervous input.


What is a binding site?

The binding site is where a specific binding molecule and a specific receptor protein can combine. This combination can only occur at the binding site. All in the 9th grade text book