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Sökning: WFRF:(Wickles Stephan)

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1.
  • Nilsson, Ola B., et al. (författare)
  • Cotranslational folding of spectrin domains via partially structured states
  • 2017
  • Ingår i: Nature Structural & Molecular Biology. - 1545-9993 .- 1545-9985. ; 24:3, s. 221-225
  • Tidskriftsartikel (refereegranskat)abstract
    • How do the key features of protein folding, elucidated from studies on native, isolated proteins, manifest in cotranslational folding on the ribosome? Using a well-characterized family of homologous α-helical proteins with a range of biophysical properties, we show that spectrin domains can fold vectorially on the ribosome and may do so via a pathway different from that of the isolated domain. We use cryo-EM to reveal a folded or partially folded structure, formed in the vestibule of the ribosome. Our results reveal that it is not possible to predict which domains will fold within the ribosome on the basis of the folding behavior of isolated domains; instead, we propose that a complex balance of the rate of folding, the rate of translation and the lifetime of folded or partly folded states will determine whether folding occurs cotranslationally on actively translating ribosomes.
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2.
  • Nilsson, Ola B., et al. (författare)
  • Cotranslational Protein Folding inside the Ribosome Exit Tunnel
  • 2015
  • Ingår i: Cell reports. - 2211-1247 .- 2211-1247. ; 12:10, s. 1533-1540
  • Tidskriftsartikel (refereegranskat)abstract
    • At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of co-translational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
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