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@ARTICLE{Wruck:892430,
      author       = {Wruck, Florian and Tian, Pengfei and Kudva, Renuka and
                      Best, Robert B. and von Heijne, Gunnar and Tans, Sander J.
                      and Katranidis, Alexandros},
      title        = {{T}he ribosome modulates folding inside the ribosomal exit
                      tunnel},
      journal      = {Communications biology},
      volume       = {4},
      number       = {1},
      issn         = {2399-3642},
      address      = {London},
      publisher    = {Springer Nature},
      reportid     = {FZJ-2021-02076},
      pages        = {523},
      year         = {2021},
      abstract     = {Proteins commonly fold co-translationally at the ribosome,
                      while the nascent chain emerges from the ribosomal exit
                      tunnel. Protein domains that are sufficiently small can even
                      fold while still located inside the tunnel. However, the
                      effect of the tunnel on the folding dynamics of these
                      domains is not well understood. Here, we combine optical
                      tweezers with single-molecule FRET and molecular dynamics
                      simulations to investigate folding of the small zinc-finger
                      domain ADR1a inside and at the vestibule of the ribosomal
                      tunnel. The tunnel is found to accelerate folding and
                      stabilize the folded state, reminiscent of the effects of
                      chaperonins. However, a simple mechanism involving
                      stabilization by confinement does not explain the results.
                      Instead, it appears that electrostatic interactions between
                      the protein and ribosome contribute to the observed folding
                      acceleration and stabilization of ADR1a.},
      cin          = {IBI-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBI-6-20200312},
      pnm          = {5352 - Understanding the Functionality of Soft Matter and
                      Biomolecular Systems (POF4-535) / 5241 - Molecular
                      Information Processing in Cellular Systems (POF4-524)},
      pid          = {G:(DE-HGF)POF4-5352 / G:(DE-HGF)POF4-5241},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33953328},
      UT           = {WOS:000656248000007},
      doi          = {10.1038/s42003-021-02055-8},
      url          = {https://juser.fz-juelich.de/record/892430},
}