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Sökning: WFRF:(Samuelsen O)

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  • Aasmundtveit, K.E., et al. (författare)
  • Structural anisotropy of poly(alkylthiophene) films
  • 2000
  • Ingår i: Macromolecules. - : American Chemical Society (ACS). - 0024-9297 .- 1520-5835. ; 33:8, s. 3120-3127
  • Tidskriftsartikel (refereegranskat)abstract
    • The structural anisotropy of various poly(alkylthiophene) films have been studied by X-ray diffraction, using both conventional methods and synchrotron radiation at grazing incidence. Solution-cast films orient with the side chains preferably normal to the film surface, whereas spin-cast films of nonstereoregular material orient with both the main and the side chains in the film plane. For thick (10-50 µm) solution-cast films, the degree of orientation depends strongly on the solvent used for casting, and on the stereoregularity of the polymer, films of stereoregular materials being more oriented than those of nonregular materials. The most oriented nonregular films are those cast from mixtures of chloroform and tetrahydrofuran. Thin (50-500 nm) solution-cast films are more oriented than the thicker ones, and the effects of different stereoregularity or different casting solvents are small. For spin-cast films, the degree of orientation is independent of substrate and solvent. Spin-cast films of stereoregular material have two different phases: One with the side chains normal to the substrate, and another where they are parallel to the substrate. The diffraction peaks of spin-cast poly(octylthiophene) narrow considerably upon heating.
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  • Elmlund, Hans, et al. (författare)
  • The cyclin-dependent kinase 8 module sterically blocks Mediator interactions with RNA polymerase II
  • 2006
  • Ingår i: Proceedings of the National Academy of Sciences of the United States of America. - : Proceedings of the National Academy of Sciences. - 0027-8424 .- 1091-6490. ; 103:43, s. 15788-15793
  • Tidskriftsartikel (refereegranskat)abstract
    • CDK8 (cyclin-dependent kinase 8), along with CycC, Med12, and Med13, form a repressive module (the Cdk8 module) that prevents RNA polymerase II (pol II) interactions with Mediator. Here, we report that the ability of the Cdk8 module to prevent pol II interactions is independent of the Cdk8-dependent kinase activity. We use electron microscopy and single-particle reconstruction to demonstrate that the Cdk8 module forms a distinct structural entity that binds to the head and middle region of Mediator, thereby sterically blocking interactions with pol II.
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  • Resultat 1-10 av 23

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