Many proteins can aggregate into amyloid fibrils. Fibril elongation has many sim

Question

Many proteins can aggregate into amyloid fibrils. Fibril elongation has many similarities to an enzymatic reaction. Experimental data on insulin amyloid-like fibril elongation suggest that the formation of fibrils follows Michaelis-Menten kinetics as shown in the below figure. A. Describe how kinetics could be experimentally measured. B. Describe how amyloid fibers follow the Michaelis-Menten enzyme kinetics. C. Describe the factors that would affect the conversion of the monomer into the fibril. D. You identify a potential inhibitor of the conversion. Describe how to identify the type of inhibition. E. Sonication is commonly used to create amyloid fibril. Suggest a hypothesis as to how sonication facilitates conversion.

Explanation / Answer

A.) Using Spectroscopic analysis the kinetics could be measured experimentally.In the spectroscopic analysis, we find the relative change in absorbance/fluorescence with time in both monomer form and the aggregate form.this relative change can be used to measure the kinetics.

B.)The rate of product formation & substrate depletion follows Michaels-menton rule wich is clearly visible if we plot a graph.this shows that the amyloid aggregate formation follows micheals-menton kinetics.

C.)Factors that affect the conversion of monomer to fibril are The concentration of substrates depletion, The concentration of product accumulation, & the Positive/negative feedback loop inhibition.

D.)After we plot a graph we can identify the type of inhibition, in a competitive inhibition we get a flat curve jbelow the curve of normal kinetics whereas the curve for non-competitive inhibition is located much lower than both of them and is sigmoid in nature. Technically a kinetic inhibition in which the maximum reaction velocity remains unchanged and Micheli's constant changes represent a competitive inhibition. and in a kinetic inhibition in which the Micheli's constant remains unchanged and the maximum reaction velocity changes represent non-competitive inhibition.

E.)Sonication is heating of proteins to break down the primary structure of the protein, to create an amyloid fibril sonication helps incomplete denaturation of the primary polypeptide sequence of protein.

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