Secondary structure of prion proteins in prion disease like Creutz feldt-Jakob disease (CJD) is
According to Wikipedia, Stanley Ben Prusine, was the first scientist to coin the term prion in 1982. It is a combination of the words Protein and Infection.
they both doesn't have nucleus Type your answer here...
You can by the typical means after trying extremely hard. Prions are unusually stable proteins, which means the normal denaturation methods (high temperature, proteases, and formalin & radiation treatments) can only reduce infectivity but not hydrolyze the structure completely. Raised temperatures will destroy normal proteins, but prions would require incredibly high temperatures and pressures that make it an ineffective treatment. The tertiary structure has been shown to be destroyed after treatment with bleach or caustic soda, or acidic substances, however.
Other modi operandi are being researched to treat prion infections and amyloids. Prions are still poorly understood and the diseases they cause are still uncurable.
At one time, cattle were fed the unwanted parts of ground up sheep. Some of those cows became infected with mad cow disease. Mad cow disease spread to humans. Cattle were also fed parts of ground up cow parts, cows eating ground up cattle were infected with that disease.
The breakthrough came in New Guinea. There, women and children would eat the brains of dead people. Men would not. Women and children would catch a disease similar to mad cow disease. Men would not. That made it obvious that the disease came from something common to women and children and not to men. Since they behaved the same as nearby groups except for eating the brains of dead people, that had to be the difference. The only difference in the brains of the dead people with mad cow disease and those without mad cow disease was the prions.
This was then tested in England where mad cow disease was common. The only difference between cows with mad cow disease and those without mad cow disease were the same prions. The people with mad cow disease had the same prions in their brains.
No. Prions are neither prokaryotic nor eukaryotic. They are similar to viruses - nonliving. However, they are more "nonliving" than viruses in the respect that they are just protein sans nucleic acid or anything cell-like.
Patients with sporadic prion diseases may have a susceptibility polymorphism in their PRNP gene, and may have spontaneous mutations forming prion proteins.