Folding of vemp into translation-arresting secondary structure is driven by the ribosome exit tunnel

HIGHLIGHTS

• who: Michal H. Kolář and collaborators from the Department of Theoretical and Computational Biophysics, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg, , Göttingen, Germany, Department of Physical Chemistry, University of Chemistry and Technology in Prague, Technická, , Prague, Czech Republic and , Department of Physics and Center for Biological Physics, Arizona State University, Tempe, AZ, USA have published the Article: Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel, in the Journal: (JOURNAL)
• what: The authors show that the VemP peptide has a low helical propensity in water and . . .
  

   

  

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