Misfolded prion proteins are involved in Fibril formation in

Misfolded prion proteins are involved in Fibril formation in diseases like Alzheimer’s disease. Your hypothesis is that when prion protein (PrP) are un glycosylated, the equilibrium shifts towards fibril formations, when prion proteins are glycosylated, the equilibrium shifts towards proper prion protein folding.

>> Explain an experiment you would do to treat this hypothesis. << THIS

(possible methods could include 2D gel electrophoresis, x-ray crystallography, 2D NMR, Isoelectric focusing, etc - not really a wrong answer here, I\'m looking for an EXPLAINATION for an experiment)

PrPe unglycosylated SH PrPsc Exposed surface Fibrils

Solution

Hypothesis- When prion protein (PrP) are un glycosylated, the equilibrium shifts towards fibril formations, when prion proteins are glycosylated, the equilibrium shifts towards proper prion protein folding.

The changes in protein folding in a glycosylated and non glycosylated protein can be studied very well using X-ray crystallography or fluorescence spectroscopy.

X - ray crystallography

This is proven to be one of the most efficient methods to determine the crystal structure in the protein folding. To do the same, the protein which has to be studied is placed inside the crystal lattice by obtaining a pure protein through supersaturation in a suitable solvent . The X- ray beams concentrate on the protein through all the directions. The image is predicted using Fourier transform . In the Fourier transform, it can easily be detected if there have been fibril formations or protein folding , as their would be definite difference in the structure of the two.