fass – -Translation – Keybot Dictionary

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«Das Protein TamA,» erklärt Fabian Gruss, Werner-Siemens-Stipendiat und Erstautor, «bildet ebenfalls ein Fass mit einer Pore. Die Pore ist mit einem Deckel nach aussen hin verschlossen, doch die Seitenwand ist einen Spalt weit geöffnet.» Wird der noch ungefaltete Autotransporter angeliefert, so angelt sich TamA ein Ende der Aminosäurekette und integriert sie nach und nach durch den Spalt in der Seitenwand in seine eigene Fassstruktur.
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“The protein TamA”, explains Fabian Gruss, first author and recipient of a Werner-Siemens PhD fellowship, “also forms a barrel with a pore. The pore is closed to the outside by a lid but a particular kink in the barrel wall provides a gate for autotransporter substrates.” When an unfolded autotransporter is delivered, TamA hooks onto one end of the substrate polypeptide chain and integrates it step by step via the gate into its own barrel structure. The TamA barrel is thus expanded; the pore widens and opens such that passenger substrates traverse to the exterior. The assembly process ends when TamA releases the autotransporter into the surrounding membrane. “The autotransporter insertion mechanism was previously completely enigmatic – for the first time, knowing the structure of TamA, we can now picture how assembly and translocation could function.”
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«Im Schutz der Chaperone wechselt FhuA ständig innerhalb tausendstel von Sekunden seine Struktur. So kann es energetisch günstige Zustände suchen, die das schrittweise Einfädeln einzelner Proteinabschnitte in die Membran erst ermöglichen.» Mit dem Einbau des letzten Abschnittes erhält FhuA dann seine reife, funktionstüchtige Fass-Struktur.
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In order to reach its goal in the outer membrane, FhuA uses the help of several chaperones. Using structural analyses and single-molecule force spectroscopy, the researchers have now elucidated how these two chaperones stabilize the immature protein and prevent misfolding. “This process is extremely dynamic,” says Hiller. “Under the protection of the chaperones, within a millisecond, FhuA constantly changes its structure. It thus explores energetically favorable conformations which enable the stepwise insertion and folding of individual protein segments into the membrane.” With the insertion of the final protein segment, FhuA acquires its mature and functional barrel structure. Left unprotected, FhuA would fold incorrectly and finally aggregate.
  Biozentrum: News Details  
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«Das Protein TamA,» erklärt Fabian Gruss, Werner-Siemens-Stipendiat und Erstautor, «bildet ebenfalls ein Fass mit einer Pore. Die Pore ist mit einem Deckel nach aussen hin verschlossen, doch die Seitenwand ist einen Spalt weit geöffnet.» Wird der noch ungefaltete Autotransporter angeliefert, so angelt sich TamA ein Ende der Aminosäurekette und integriert sie nach und nach durch den Spalt in der Seitenwand in seine eigene Fassstruktur.
Compare text pagesCompare HTM pagesOpen source URLOpen target URLDefine biozentrum.unibas.ch as primary domain
“The protein TamA”, explains Fabian Gruss, first author and recipient of a Werner-Siemens PhD fellowship, “also forms a barrel with a pore. The pore is closed to the outside by a lid but a particular kink in the barrel wall provides a gate for autotransporter substrates.” When an unfolded autotransporter is delivered, TamA hooks onto one end of the substrate polypeptide chain and integrates it step by step via the gate into its own barrel structure. The TamA barrel is thus expanded; the pore widens and opens such that passenger substrates traverse to the exterior. The assembly process ends when TamA releases the autotransporter into the surrounding membrane. “The autotransporter insertion mechanism was previously completely enigmatic – for the first time, knowing the structure of TamA, we can now picture how assembly and translocation could function.”