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![[Figure 4]](id5003fig4mag.jpg)
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Figure 4
The participation of ribosome in co-translational protein folding. (a) An mRNA template with synonymous codons (in black) often includes substituted rare-codon clusters (in pink) near the 3′ end. Ribosomes (dark grey) progressively translate (indicated by black arrows) NCs using this mRNA template until they encounter the rare-codon segment, where they pause (ribosome in colour with a red cross). The paused ribosome state (boxed) provides time for the emerged NC (in red) to undergo folding. (b) An NC sequence (shown in green) can interact with the ribosome surface inside and on the outside surface (highlighted in pink circles), which can help NCs to avoid misfolding. (c) Several ribosome-associating factors (RAFs) bind to the ribosome co-translationally and interact with the emerging NC (only bacterial RAFs are shown). N-terminal processing RAFS (PDF, magenta; MAP, purple) bind to the ribosome near the exit port of the 50S. Similarly, chaperones such as SRP (in orange; RNA in black) and TF (in blue) bind near the 50S exit port to assist co-translational translocation and folding, respectively. |
![[Figure 4]](id5003fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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