The ribosome lowers the entropic penalty of protein folding
The study in Nature reveals that the ribosome reduces the entropic penalty of protein folding, facilitating active conformations and protecting nascent chains from misfolding, highlighting its role in protein evolution.
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The study published in Nature investigates how the ribosome influences protein folding during biosynthesis. It reveals that the ribosome lowers the entropic penalty associated with protein folding by structurally expanding the unfolded nascent chain and increasing its solvation. This entropic destabilization can reduce the folding penalty by up to 30 kcal/mol, facilitating the formation of partially folded intermediates essential for some proteins to achieve their active conformations. The research utilized paramagnetic relaxation enhancement (PRE) NMR spectroscopy and molecular dynamics simulations to analyze the unfolded state of a model protein both on and off the ribosome. The findings indicate that the ribosome not only alters the thermodynamic stability of nascent chains but also protects them from mutation-induced unfolding, suggesting a significant role in protein evolution. The study highlights the distinct thermodynamic properties of co-translational folding compared to traditional in vitro refolding, emphasizing the ribosome's critical role in ensuring proper protein folding and function.
- The ribosome reduces the entropic penalty of protein folding by expanding the unfolded nascent chain.
- This reduction can facilitate the formation of partially folded intermediates necessary for active protein conformations.
- The study utilized advanced NMR spectroscopy and molecular dynamics simulations to analyze protein folding dynamics.
- Ribosome interactions help protect nascent chains from misfolding and mutation-induced unfolding.
- The findings underscore the importance of co-translational folding in maintaining protein stability and function.
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The ribosome lowers the entropic penalty of protein folding (Nature)
A study in Nature reveals that the ribosome reduces the entropic penalty of protein folding, facilitating co-translational folding and protecting nascent chains from mutations, enhancing protein stability and evolution.
2 commentsHere 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.
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