Discriminating taste of prions

Article Abstract:

The mechanisms underlying the conversion of yeast prion proteins to an infectious form are clarified. Researchers have used an array assay for analyzing the ability of the amino-acid sequences to bind and to modify the full-length protein and have concluded that the small elements of the Sup35 amino-acid sequence can recognize soluble conformations of the protein with unusual specificity, which is sufficient for converting the soluble proteins to the abnormal prion state.

Analysis, Conformational analysis, Amino acid sequence, Amino acid sequencing

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Prions and their partners in crime

Article Abstract:

Prions, the infectious agents of transmissible spongiform encephalopathies (TSEs), lack nucleic acids and are composed of a pathological, self-inducing form of the host's prion protein (PrP). Interactions between TSE-associated PrP and its normal counterpart are also pathologically important, so the physiological functions of normal PrP and how they might be corrupted by TSE infections are investigated.

Montana, Causes of, Genetic aspects, Prion diseases, Host-parasite relationships

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Designer prions

Article Abstract:

The design of prion based on the aggregation properties of tracts of glutamine amino acids is discussed. The asparagine or glutamine rich region is essential for aggregation.

Amino acids, Chemical properties

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