Prions are naturally synthesized glycoproteins.  They contain two carbohydrate chains and a lipid base which connects to the protein portion of the cell membranes of nervous tissue.  A unique characteristic to all forms is one which may have deadly consequences.  When the structure of a single protein becomes misfolded, it has the ability to cause other prion proteins to change from their normal structure to that which is misfolded eventually affecting the entity of an organism.  One prion of considerable study is the protein PrP which, due to a genetic predisposition, infrequently sporadically becomes misfolded thus causing others to alter their normal structural state changing the protein to that called PrP^sc.  In addition to spontaneous misfolding, PrP^sc prions can be acquired through injestion of meat containing the altered proteins as well as through blood contact via an exposed wound.  PrP^sc is denoted as the specific cause of such diseases as bovine spongiform encephalopathy or mad-cow disease and human spongiform encephalopathy or Creutzfeldt-Jakob disease.  A PrP prion consists of many α-heli and upon misfolding to PrP^sc the alteration results in a molecule containing many β-pleated sheets.  The PrP^sc prions are phagocytized by immunal macrophages after recognition of its pathogenicity and travel through the body intended to be deposited in the lymphnodes where they would be denatured.  However, upon contact with nervous tissue along the way they adhere and can then travel up the corresponding nerve into the brain.  This causes the formation of long fibrils and insoluble plaques affecting the functioning of the brain.  Studies on these prions are conducted using nuclear magnetic resonance spectroscopy.