670 karma · joined December 22, 2018
It's discouraging to see these on HN and then realize that most never go anywhere, or are so far out you may not see it in your lifetime.
Maybe we should flag anything not already in a phase 3 trial :)
It's great that there are folks like you preserving this history
I always tried to treat and see it as a teaching and learning exercise and not make it accusatory or negative. As a reviewer, see it as an opportunity to teach others in good code practices. As a reviewee, see it as an opportunity to learn, not as a slam on you personally.
Doesn't solve it completely, but it helps.
Here is a rewritten version of the passage at a 10th-grade reading level:
Most proteins begin to fold into their proper shapes while they are being made on the ribosome. Studies have shown that the way proteins fold during this process, and the energy involved, can be very different from how they fold when they are refolded outside of this process. Until now, it wasn't clear why the ribosome affects protein folding in this way.
In this study, we looked at the detailed structures of an unfolded protein both on and off the ribosome. We found that the ribosome causes the unfolded protein chain to spread out more and increases how much it interacts with water. This makes the protein chain less stable when it's on the ribosome compared to when it's alone. Tests using 19F NMR confirmed that this instability makes it easier for the protein to start folding on the ribosome, lowering the energy cost by up to 30 kcal/mol. This helps the protein form partially folded shapes, which are necessary for some proteins to reach their active forms. These effects also help protect the protein from unfolding due to mutations, suggesting that the ribosome plays an important role in how proteins evolve. By linking the structure and movement of the protein chain to how it folds and behaves after folding, our findings explain why protein folding on the ribosome is different from folding after translation is complete.