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Thus, ‘There is no information transfer from protein to nucleic acid’, postulates the Central Dogma.

This postulate is not based on any physical law (in principle, all reactions involved in translation are reversible) but rather on the design of the translation system that hampers reverse translation.

Regardless of the exact mechanisms, prions clearly violate the Central Dogma by enabling the information flow from proteins to the genome.

The agents of these diseases showed extremely unusual properties, in particular extraordinary resistance to treatment that inactivates even the smallest nucleic acid molecules such as high-dose UV irradiation [].

The history of research on the agents of spongiform encephalopathies involved numerous false leads in the persistent quest for a conventional virus or an unusual nucleic acid-containing agent linked to these diseases [].

Eventually, a series of meticulous experiments by Prusiner and colleagues (winning the 1997 Nobel Prize in Physiology or Medicine) has demonstrated beyond doubt that an iconoclastic hypothesis originally proposed by Griffith [].

The amyloid-forming conformer possesses self-propagating properties: once a prion molecule assumes this conformation, it interacts with other molecules in the soluble conformation and induces their conversion to the amyloid-forming conformation, much like Ice-9 in Kurt Vonnegut’s A seminal discovery that greatly facilitated further study of prions was the demonstration that prions exist not only in animals but also in yeast where they mediate epigenetic inheritance of phenotypic traits [].

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