Sometimes we are forced to see things differently. But it is never easy because we are creatures of habit and, like it or not, shackled by what we were first led to believe. This is exactly what happened with the prion. Prions are proteins whose shape can change under certain conditions, and in so doing be at the heart of fatal diseases. Many afflictions are caused by a change in a protein's 3D structure, so this can hardly be considered a pioneering concept in the world of molecular biology. What is relatively new, however, is the notion that a protein can be the actual cause of infection. An infection is defined by an entity able to transmit, from one organism to another or indeed one cell to another, the information it needs to thrive and propagate. Viruses and bacteria infect organisms by multiplying inside them, killing off cells as they do so and causing havoc in their wake - such as meningitis, the classic flu or AIDS. Some prion proteins, once their shape has changed, are able to behave in the same way and cause neurodegenerative illnesses such as scrapie in sheep and Creutzfeld-Jakob disease in humans for instance. Recently, a prion of a different nature was discovered: one that refuses to change shape. Its name is PrP V127.
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Snapshot : awa1 and hpf1
When we raise a glass of wine, rarely do we give a thought to what has been involved in its making. Yet a wine's hue, its taste, its aroma, its sparkle and even the nature of its haze are given the same attention a mother would to her newborn. Many of the qualities of a wine are the doings not only of proteins inherent to the grapes, rice or any other product used to make it, but also to proteins which belong to yeast strains that are added for fermentation, and hence the production of alcohol. Two such proteins are AWA1 and HPF1. AWA1 is involved in the production of foam as the Japanese rice wine - sake - is brewed, and HPF1 in the production of haze in white wine. And both proteins belong to the cell wall of different strains of Saccharomyces cerevisiae.
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