What makes nerve proteins “want” to copy the folding patterns of prions, causing prion diseases?

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I understand that prions are misfolded in a way that’s smaller and more spatially efficient than the normal proteins that brain tissue is made out of, and the spread of these smaller proteins causes the tissue to shrink and literally grow holes. What I don’t understand is why the proteins in an infected brain “want” to copy the improper fold pattern – they aren’t sentient, they can’t notice the pattern and think “Why didn’t I try folding like this before, it’s so much more efficient”. If proteins “want” to fold a certain way because of a physical property, what was stopping them from folding that way in the first place? What is it about the introduction of a prion that makes healthy nerve tissue “get the idea” to fold that way?

In: Biology

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Anonymous 0 Comments

Proteins get folded in a way that is locally stable, but there could be a more stable conformation that the protein could fold into if the conditions are right. Prions nudge healthy proteins into this other state.

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