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Sökning: WFRF:(Jaeger Franziska)

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1.
  • Debatin, Franziska, et al. (författare)
  • An Isoreticular Family of Microporous Metal-Organic Frameworks Based on Zinc and 2-Substituted Imidazolate-4-amide-5-imidate : Syntheses, Structures and Properties
  • 2012
  • Ingår i: Chemistry - A European Journal. - : Wiley. - 0947-6539 .- 1521-3765. ; 18:37, s. 11630-11640
  • Tidskriftsartikel (refereegranskat)abstract
    • We report on a new series of isoreticular frameworks based on zinc and 2-substituted imidazolate-4-amide-5-imidate (IFP-14, IFP=imidazolate framework Potsdam) that form one-dimensional, microporous hexagonal channels. Varying R in the 2-substitued linker (R=Me (IFP-1), Cl (IFP-2), Br (IFP-3), Et (IFP-4)) allowed the channel diameter (4.01.7 angstrom), the polarisability and functionality of the channel walls to be tuned. Frameworks IFP-2, IFP-3 and IFP-4 are isostructural to previously reported IFP-1. The structures of IFP-2 and IFP-3 were solved by X-ray crystallographic analyses. The structure of IFP-4 was determined by a combination of PXRD and structure modelling and was confirmed by IR spectroscopy and 1H MAS and 13C CP-MAS NMR spectroscopy. All IFPs showed high thermal stability (345400?degrees C); IFP-1 and IFP-4 were stable in boiling water for 7 d. A detailed porosity analysis was performed on the basis of adsorption measurements by using various gases. The potential of the materials to undergo specific interactions with CO2 was investigated by measuring the isosteric heats of adsorption. The capacity to adsorb CH4 (at 298 K), CO2 (at 298 K) and H2 (at 77 K) at high pressure were also investigated. In situ IR spectroscopy showed that CO2 is physisorbed on IFP-14 under dry conditions and that both CO2 and H2O are physisorbed on IFP-1 under moist conditions.
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3.
  • Rollauer, Sarah E., et al. (författare)
  • Structure of the TatC core of the twin-arginine protein transport system
  • 2012
  • Ingår i: Nature. - : Springer Science and Business Media LLC. - 0028-0836 .- 1476-4687. ; 492:7428, s. 210-
  • Tidskriftsartikel (refereegranskat)abstract
    • The twin-arginine translocation (Tat) pathway is one of two general protein transport systems found in the prokaryotic cytoplasmic membrane and is conserved in the thylakoid membrane of plant chloroplasts. The defining, and highly unusual, property of the Tat pathway is that it transports folded proteins, a task that must be achieved without allowing appreciable ion leakage across the membrane. The integral membrane TatC protein is the central component of the Tat pathway. TatC captures substrate proteins by binding their signal peptides. TatC then recruits TatA family proteins to form the active translocation complex. Here we report the crystal structure of TatC from the hyperthermophilic bacterium Aquifex aeolicus. This structure provides a molecular description of the core of the Tat translocation system and a framework for understanding the unique Tat transport mechanism.
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  • Resultat 1-3 av 3

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