The goal of the research is to use the bioinformatics and homology model to obtain three dimensional native and mutated PMP22 models, and show how it is anchored to the cell membrane to determine how L16P and T118M mutation affect the conformational behavior of PMP22.
The conclusion obtained in the experiment tells that there is less stability with mutated protein compared to the normal proteins, resulting specifically from residue 16 and in alpha-helix h1-h2. The data obtained in the experiment also concluded that there was less hydrogen bonding at the side near the mutated site and as a result of this deviation from the normal protein, the mutated protein has a harder time getting out of the ER.
The impact on the disease is that when the structure and how the protein complex interacts, it would make the mechanism of the disease easier to understand, and by understanding the mechanism of the disease at a molecular level, a relatively noninvasive treatment can be created to combat the effect of mutated proteins.
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