Prions
normally exist as cellular membrane proteins. In humans, 209 amino acids with
one disulfide bond form a primarily alpha-helical prion protein structure with
a molecular mass of 35 to 36 kDa. The native prion protein exists in this stateand appears likely to play a role in cell-cell adhesion and intracellular
signaling leading to cell-cell communication within the brain.
The specific
role and function of the prion protein elude research efforts and remains a
controversial topic. In addition, early and definitive diagnosis of the
infection remains difficult. According to the protein only theory, variations
in the protein structure and resistance to proteases may cause infectious diseases
leading to encephalopathy. Misfolding of the native prion protein leads to a
protein’s structure that increases the proportion of alpha-helices to
beta-sheets.(Read More)
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