"What we've done is to reveal the mechanics behind the trick." But how exactly they do their work has been poorly understood: "The chaperones do some kind of magic," says Alexandra Pozhidaeva, co-lead author of the paper who contributed to this study as a postdoctoral research associate at UMass Amherst and is currently a postdoctoral fellow at UConn Health. These "chaperones" can figure out which proteins are at risk of being deformed and can then lend that protein additional help. Researchers have long known that special molecules called chaperones help shepherd the protein into its final, correct shape. The protein folding process, during which a chain of amino acids assumes its final shape as a protein, can be especially fraught. Luckily, cells rely on a rigorous quality control to offset the devastating consequences. But when something goes awry, the results can be catastrophic. Most of the time, this process works flawlessly, and our cells can build and reproduce themselves smoothly. Through the complex processes of transcription, followed by protein synthesis and finally protein folding, those four, two-dimensional letters turn into a 20-letter, three-dimensional recipe for proteins. There are four "letters" in the linear DNA code: A, C, G and T.
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