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Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel
View ORCID ProfileMichal H. Kolář, View ORCID ProfileGabor Nagy, John Kunkel, Sara M. Vaiana, View ORCID ProfileLars V. Bock, View ORCID ProfileHelmut Grubmüller
doi: https://doi.org/10.1101/2021.04.15.440051
Michal H. Kolář
†Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
¶University of Chemistry and Technology, Technicka 5, 16628 Prague, Czech Republic
Gabor Nagy
†Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
John Kunkel
‡Department of Physics and Center for Biological Physics, Arizona State University, 85287 Tempe, AZ, USA
Sara M. Vaiana
‡Department of Physics and Center for Biological Physics, Arizona State University, 85287 Tempe, AZ, USA
Lars V. Bock
†Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
Helmut Grubmüller
†Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany
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Posted April 15, 2021.
Folding of VemP into translation-arresting secondary structure is driven by the ribosome exit tunnel
Michal H. Kolář, Gabor Nagy, John Kunkel, Sara M. Vaiana, Lars V. Bock, Helmut Grubmüller
bioRxiv 2021.04.15.440051; doi: https://doi.org/10.1101/2021.04.15.440051
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