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Sometimes they seem to misfold all on their own.
Prions can also misfold on their own accord and give rise to disease.
Environmental stress can cause proteins to misfold and aggregate.
Sometimes, for reasons of inheritance or circumstance, the origami goes wrong and they misfold.
Cellular stresses, such as increased temperature, can cause proteins in the cell to misfold.
This causes the protein to spontaneously misfold and form aggregates.
In the amyloid diseases, something was causing normal proteins to misfold.
Prions spread across the brain by causing other copies of the same protein to misfold.
Folding@home's goal is to understand why proteins "misfold."
Something causes one protein to misfold and present the wrong greeting to a passing protein.
The exposure to ultra fine air pollution also caused proteins to misfold, rendering them dysfunctional.
These repeats in huntingtin are what cause it to misfold, eventually leading to neuron death and the symptoms of the disease.
Somehow, the theory goes, prions force normal proteins to misfold, setting off a destructive chain reaction in the brain.
For reasons that are not well understood, some proteins have a tendency to misfold into a second shape involving long sheets that stick together.
The 1997 discovery that mHtt fragments misfold led to the discovery of the nuclear inclusions they cause.
The misshapen protein, called an infectious prion, causes other healthy proteins to misfold in a chain reaction.
However, due to a protein's chemical properties or other factors, proteins may misfold - that is, fold down the wrong pathway and end up misshapen.
Misfolded proteins cause other proteins to misfold, then they die, as do the unfortunate creatures afflicted by them.
Because proteins share a common structural feature known as the polypeptide backbone, all proteins have the potential to misfold under some circumstances.
In Alzheimer's and other diseases, certain proteins misfold and form lethal aggregate deposits known as 'amyloids'.
However, newly synthesized proteins may not fold correctly, or properly folded proteins can spontaneously misfold.
In addition, the more stress that a cell feels from misfolded proteins the more probable new proteins will misfold.
They can use these MSMs to reveal how proteins misfold and to quantitatively compare simulations with experiments.
When a misfolded prion comes into contact with a healthy prion, it can cause the healthy proteins to misfold.
Moreover, the theory holds, the misfolded protein acts like a seed crystal, causing other, healthy proteins to misfold and bringing on destruction of brain tissue.