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The binding of calcium to which molecule causes the myosin binding sites to be exposed?
Troponin binds to the Calcium ions to expose the actin to the myosin heads.
How does an increase in intracellular calcium cause a muscle fiber to contract?
An increase in intracellular calcium concentration triggers muscle contraction by binding to troponin, a regulatory protein on the actin filaments. This binding causes a conformational change that moves tropomyosin away from the myosin-binding sites on actin, allowing myosin heads to attach to actin. The myosin heads then pivot, pulling the actin filaments inward and resulting in muscle contraction through the sliding filament mechanism. Ultimately, this process is regulated by the calcium levels within the muscle fiber.
Does Tropomyosin molecules move and expose specific sites on myosin filaments?
Yes, tropomyosin molecules block specific binding sites on actin filaments in relaxed muscle. When calcium ions bind to troponin, it causes a conformational change in tropomyosin, exposing the binding sites on actin, which allows myosin heads to bind and initiate muscle contraction.
What enzymes do myosin heads have?
Myosin heads contain ATPase enzymes, which hydrolyze ATP to provide energy for muscle contraction. This energy is used to power the movement of myosin heads along actin filaments during the sliding filament theory of muscle contraction.
What protein with heads that attach in cross bridging?
myosin
Binding of the myosin heads sequentially prevents what?
myosin crossbridge binding
The binding of calcium to which molecule causes the myosin binding sites to be exposed?
Troponin binds to the Calcium ions to expose the actin to the myosin heads.
What molecule has a binding site for myosin heads?
Actin is the molecule that has a binding site for myosin heads. This interaction is crucial for muscle contraction as myosin binds to actin and generates force to cause muscle movement.
What is needed to attach and detach myosin heads from actin?
For attachment of myosin heads to actin, calcium ions must bind to troponin, causing tropomyosin to move out of the way, exposing the binding site on actin. ATP then binds to the myosin head, leading to its activation and attachment to actin. For detachment, ATP is hydrolyzed, causing a conformational change in the myosin head that releases it from actin.
What does the release of ADP and P from the myosin head cause?
The release of ADP and P from the myosin heads causes the myosin heads to change shape.
How does an increase in intracellular calcium cause a muscle fiber to contract?
An increase in intracellular calcium concentration triggers muscle contraction by binding to troponin, a regulatory protein on the actin filaments. This binding causes a conformational change that moves tropomyosin away from the myosin-binding sites on actin, allowing myosin heads to attach to actin. The myosin heads then pivot, pulling the actin filaments inward and resulting in muscle contraction through the sliding filament mechanism. Ultimately, this process is regulated by the calcium levels within the muscle fiber.
What makes rigormortis cease after 72 hours?
The myosin heads detach from actin, allowing the muscles to relax; prior to rigor mortis, Directly after death ATP is not produced therefore, Ca +2 is absent within the myosin binding sites on the actin, which leads to the myosin heads not being able to detach from actin, this condition doesnt allow the muscle to relax, aka rigor mortis. For the muscle to relax or for rigor mortis to cease the myosin heads detach from actin.
What is another name for Myosin heads?
globular heads
What are myosin heads?
Cross-bridge
What prevents actin myofilaments from sliding backward when a myosin head releases?
During contraction, there are always some myosin heads attached to the actin myofilament when other myosin heads are detaching.
What do muscle fibers need to reset the myosin heads?
ATP binds myosin, allowing it to release actin and be in the weak binding state (a lack of ATP makes this step impossible, resulting in the rigor state characteristic of rigor mortis). The myosin then hydrolyzes the ATP and uses the energy to move into the "cocked back" conformation.
Does Tropomyosin molecules move and expose specific sites on myosin filaments?
Yes, tropomyosin molecules block specific binding sites on actin filaments in relaxed muscle. When calcium ions bind to troponin, it causes a conformational change in tropomyosin, exposing the binding sites on actin, which allows myosin heads to bind and initiate muscle contraction.
