Abstract
The mammalian prion PrPSc causes fatal neurodegenerative ailments in humans and farm animals. The molecular mechanisms of its propagation and transmissibility between species will not be understood until sufficient knowledge of its structure is gathered. This task has been hampered by the insoluble nature of PrPSc, which renders classic techniques, such as nuclear magnetic resonance or x-ray crystallography, unusable. However, a number of alternative approaches, such as limited proteolysis, electron microscopy and Fourier transform infrared spectroscopy, have yielded valuable low-resolution structural information. Pieced together, these data present PrPSc as a stackable molecule whose core is probably a β-solenoid formed by two or three rungs of short β-strands interspersed with numerous loops and turns. A reasonable understanding of its architecture might soon be achieved.
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