Effects of Low PH on Respiratory Muscle Fibers Discussion

Please answer the 2 discussion questions in two separate papers:

Discussion Question 1:

Cystic fibrosis is genetic disease caused by mutations in the CFTR gene. The consequence of this is production of an abnormal transmembrane protein that is responsible for producing sweat, mucus, and digestive fluids.

Explain in depth the correlation between the defective gene and the abnormal protein that is produced. Be sure to mention the process involved in protein production, whether or not those process(s) have properly occurred, and their end products.

Provide details in your explanation and support your answer with facts from your textbook, research, and articles from scholarly journals. Remember to add references in APA format at the end of your post to avoid plagiarism.

Discussion Question 2:

A depressed person attempts to commit suicide by taking a whole bottle of sleeping pills. The pills cause a drastic decrease in the pH. The patient starts having breathing difficulties because the thick and thin filaments within the respiratory muscles are breaking down.

Explain in depth the correlation between the person’s pH and why their respiratory muscles are breaking down.

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Provide details in your explanation and support your answer with facts from your textbook, research, and articles from scholarly journals. Remember to add references in APA format at the end of your post to avoid plagiarism.

Acidosis (low pH) is the oldest putative agent of muscular fatigue, but the molecular mechanism underlying its depressive effect on muscular performance remains unresolved. Therefore, the effect of low pH on the molecular mechanics and kinetics of chicken

skeletal muscle myosin was studied using in vitro motility (IVM) and single molecule laser trap assays. Decreasing pH from 7.4 to 6.4 at saturating ATP slowed actin filament velocity (V_actin) in the IVM by 36%. Single molecule experiments, at 1 μM ATP, decreased the average unitary step size of myosin (d) from 10 ± 2 nm (pH 7.4) to 2 ± 1 nm (pH 6.4). Individual binding events at low pH were consistent with the presence of a population of both productive (average d = 10 nm) and nonproductive (average d = 0 nm) actomyosin interactions. Raising the ATP concentration from 1 μM to 1 mM at pH 6.4 restored d (9 ± 3 nm), suggesting that the lifetime of the nonproductive interactions is solely dependent on the [ATP]. V_actin, however, was not restored by raising the [ATP] (1–10 mM) in the IVM assay, suggesting that low pH also prolongs actin strong binding (t_on). Measurement of t_on as a function of the [ATP] in the single molecule assay suggested that acidosis prolongs t_on by slowing the rate of ADP release. Thus, in a detachment limited model of motility (i.e., V_actin ∼ d/t_on), a slowed rate of ADP release and the presence of nonproductive actomyosin interactions could account for the acidosis-induced decrease in V_actin, suggesting a molecular explanation for this component of muscular fatigue.

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