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

Kolár, Michal H; Nagy, Gabor; Kunkel, John; Vaiana, Sara M; Bock, Lars V; Grubmüller, Helmut

Kolár, Michal H; Nagy, Gabor; Kunkel, John; Vaiana, Sara M; Bock, Lars V; Grubmüller, Helmut.

Afiliación

Kolár MH; Department of Theoretical and Computational Biophysics, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, 370 77 Göttingen, Germany.
Nagy G; Department of Physical Chemistry, University of Chemistry and Technology in Prague, Technická 5, 166 28 Prague, Czech Republic.
Kunkel J; Department of Theoretical and Computational Biophysics, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, 370 77 Göttingen, Germany.
Vaiana SM; Department of Physics and Center for Biological Physics, Arizona State University, Tempe, AZ 85287, USA.
Bock LV; Department of Physics and Center for Biological Physics, Arizona State University, Tempe, AZ 85287, USA.
Grubmüller H; Department of Theoretical and Computational Biophysics, Max Planck Institute for Multidisciplinary Sciences, Am Fassberg 11, 370 77 Göttingen, Germany.

Nucleic Acids Res ; 50(4): 2258-2269, 2022 02 28.

Article en En | MEDLINE | ID: mdl-35150281

Asunto(s)

Peptidil Transferasas; Ribosomas; Péptidos/metabolismo; Peptidil Transferasas/metabolismo; Biosíntesis de Proteínas; Pliegue de Proteína; Estructura Secundaria de Proteína; Proteínas/metabolismo; Ribosomas/metabolismo; Agua/metabolismo

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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ribosomas / Peptidil Transferasas Idioma: En Revista: Nucleic Acids Res Año: 2022 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Reino Unido

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