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by subungual
1913 days ago
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So denaturing a protein generally involves interfering with the noncovalent interactions (e.g. hydrogen bonds, attractions between internal charges) that allow it to fold into the right functional shape. Often times, these proteins folded under conditions that carefully facilitated their coming out the right way, so simply removing the denaturing stimulus (e.g. allowing them to cool) won't result in a reversion to their former configuration. This is what you see, for example, in cooking, where there's a discrete change that doesn't revert. Prions are generally much more stable and can revert back to dangerous form once denaturing conditions change back. It takes a lot more to denature them irreversibly than it does most proteins. This stability is part of what makes them so dangerous and difficult to remove. |
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Indeed I'd imagine that almost definitionally prions must be difficult to denature. Since they are non-living and therefore have no way of "seeking out food," durability is the only way they can compete for reproduction. That is they can only become infectious if their resistance to denaturing was sufficiently high to resist environmental damage until their next target comes around.