Papers on "Isolation and Purification of Muscle Proteins" and similar term paper topics

Paper #103275 :: Isolation and Purification of Muscle Proteins
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This paper discusses the isolation and purification of actin and myosin in skeletal myofibrils.

Written in 2008; 1,791 words; 7 sources; APA; $ 57.95

Paper Summary:

The writer explains that in the set of experiments discussed in the paper, myosin and actomyosin were isolated and gradually purified from rabbit muscle myofibrils. The two proteins were initially precipitated together out of solution, in order to remove any impurities. Then, the two proteins could be separated from each other, by taking advantage of differential solubility. The writer notes that after each time they were re-suspended or redissolved, the solutions were centrifuged in order to further improve purity. Any solution containing the contractile proteins or ATP were kept on ice during the experiments, and stored in a freezer at all other times. The writer discusses that using the Bradford protein assay and the SDS-PAGE, the concentrations and weights of the purified proteins in the final solutions were measured. For all protein samples, no appreciable concentration of protein could be detected after diluting the samples by 100 times. However, the other two dilutions yielded normal results.

Outline:
Abstract
Introduction
Materials and Methods
Results
Discussion

From the Paper:

"The head of the myosin is the part which interacts with the other molecules. Without ATP, the myosin head is bound tightly to the actin, called the rigor state. However, ATP weakens this interaction by opening a cleft in the myosin head and disrupting the actin-binding site. When the myosin head is free of actin, it hydrolyzes ATP to ADP. This causes a conformational change in the head that moves it to a new position, closer to the (+) end of the actin filament, (away from the origin site) where it reattaches. The dissociation of the phosphate from ATP also causes a conformational change, this time in the myosin head. As a result, myosin returns to its original state (the rigor state). Because myosin is still bound to actin, this conformational change exerts a force that causes myosin to move the actin filament. This is the power stroke. Essentially, contraction is a series of these power strokes by the actomyosin complex, the myosin head is moving along the actin filament through constant detachment and reattachment."

Tags: molecular dilutions calcium ATP

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