The sarcoplasmic reticulum is the specialized organelle of the muscle cells that allows for calcium to be sequestered. Once calcium is released into the cytoplasm it interacts with troponin and tropomyosin, allowing myosin and actin to bind and cause contraction. Calcium must be sequestrated to allow for the myosin-actin bridges to be broken and reset for future contraction.

The sarcolemma is the muscle cell membrane. The T-tubules permeate the muscle cell to allow for propagation of the stimulating action potential to all parts to the cell. The sarcomeres are the contractile units of the muscle cell.

Keep in mind that muscle cells do not undergo mitosis. Instead, the increase in muscle size is due to increased muscle fiber diameter. The number of sarcomeres and mitochondria in each muscle fiber will also increase over time. This increase in size, but not cell number, is called hypertrophy.

The proteins troponin and tropomyosin are attached to the actin filaments in sarcomeres. These proteins function to block the myosin-binding site on the actin protein, preventing unnecessary contraction. When calcium is released from the sarcoplasmic reticulum, it will attach to troponin. The troponin will then pull tropomyosin away from the actin filament, which allows myosin heads to attach and cause a contraction.

ATP binds myosin to release it from the actin binding site and is converted to ADP in order to adjust the myosin head to a high-energy position.

Muscle contraction is very tightly regulated. Tropomyosin binds actin filaments and covers the myosin binding sites. Troponin interacts with tropomyosin. When stimulated by calcium, troponin undergoes a conformational change that moves the tropomyosin and exposes the myosin binding sites on the actin protein. When the binding sites are exposed myosin can bind actin and muscle contraction can occur. Troponin does not bind myosin or actin directly, and it does not get ubiquinated and degraded.

Muscle contraction is regulated by blocking the myosin binding sites of actin and selectively exposing them when contraction is supposed to occur. Tropomyosin binds actin fibers and recruits troponin to perform this blocking function. Troponin will bind calcium ions, change conformation, and move tropomyosin out of the way of the myosin binding sites to allow contraction to occur. The most likely mutation described in the question is one that causes troponin to have a decreased affinity for calcium, thus never allowing the myosin binding sites to be exposed under normal physiological concentrations.

The question states that muscle cramps occur because myosin heads remain attached to the active site on actin; therefore, you are looking for a molecule that is responsible for the detachment of the myosin head from actin. Recall that binding of ATP to the myosin head releases the myosin head from the actin binding site. This allows tropomyosin to re-attach to actin and causes the muscle to relax. The ATP that is bound to the myosin head dissociates into ADP and inorganic phosphate, allowing the myosin head to enter its high-energy state and prepare for another contractile stroke. Once tropomyosin is released again from the actin filament, the ADP and inorganic phosphate on the myosin head are released, the myosin head attaches to actin, and the cycle continues.

Calcium is essential for muscle contraction because it allows for the removal of tropomyosin from the actin binding sites. Depletion of calcium, however, would cause the actin sites to be blocked, preventing contraction from occurring (as opposed to the sustained contraction of a muscle cramp). Depleted sodium may result in fewer action potentials at the neuromuscular junction. This would also inhibit muscle contraction, rather than sustain it. Muscular microtears can occur during exercise, but are unrelated to muscle cramps.

Troponin and tropomyosin are both proteins that play a big role in muscle contraction. Since they are proteins, troponin and tropomyosin are made up of amino acids. Recall that fatty acids make up lipids, not proteins. 

During a typical muscle contraction, tropomyosin is bound to actin. This blocks the binding of the myosin head to actin and prevents muscle contraction. When calcium ions are released from the sarcoplasmic reticulum, troponin interacts with actin and removes tropomyosin. Neither protein directly interacts with myosin. Tropomyosin is very important because it prevents prolonged muscle contraction which can lead to several muscle disorders.

ATP has a huge role in muscle contraction; however, it never interacts with tropomyosin. ATP is important to remove the myosin head from the active site on actin. Upon ATP binding, the myosin head detaches itself from actin, which allows tropomyosin to re-attach to the active site on actin. Without ATP, myosin heads can’t detach themselves from actin and prolonged muscle contraction occurs. After death a person stops producing ATP; therefore, contracted muscles can’t relax and rigor mortis ensues.

In a typical muscle cell, tropomyosin is bound to an active site on actin. This prevents muscle contraction because the myosin head cannot bind to actin active site. Muscle contraction is initiated when the sarcoplasmic reticulum releases calcium ions into the cytoplasm of the muscle cell. Calcium ions bind to and activate troponin. Activated troponin molecules subsequently remove tropomyosin from the active site on actin. This allows muscle contraction to occur because the myosin head can now bind to the active site on actin and initiate a power stroke to shorten the sarcomere.

An individual with depleted calcium ions in his sarcoplasmic reticulum will not activate troponin and, therefore, will have reduced muscle tone and strength.

The sarcoplasmic reticulum is responsible for the storage of calcium ions that are used in muscle contraction. Prior to a contraction, an action potential will reach the sarcoplasmic reticulum, making it permeable to calcium ions. At the end of the contraction, the sarcoplasmic reticulum will actively pump calcium ions back into its lumen.

The sarcoplasmic reticulum is not involved in protein synthesis.

Calcium plays a huge role in the regulation of muscle contraction. Without the presence of calcium, the myosin binding sites on the actin filaments are blocked by tropomyosin and muscle contraction cannot occur. Stimulation from the nervous system causes a chain reaction that releases large stores of calcium from the sarcoplasmic reticulum to regulate muscle contraction.

Sodium ions play an essential role in initiating the chain reaction that eventually leads to calcium release, but is not stored in the sarcoplasmic reticulum. Potassium plays a role in regulating membrane potential, but also is not stored in the sarcoplasmic reticulum. Protons are essential to mitochondrial function and play a crucial role in myocyte metabolism, but are not linked to the sarcoplasmic reticulum or contractile function.