The authors report about the formation of Al4Cu9 from a thin Cu film evaporated on the five‐fold surface of icosahedral AlPdMn. By heating up to 350°C Al diffuses from the quasicrystal into the Cu film forming well crystalline Al4Cu9 present in 5 domains rotated by 72° with respect to each other and exposed in the (110) surface. The investigation was performed using Low Energy Electron Diffraction, X‐ray Photoelectron Diffraction and X‐ray Photoelectron Spectroscopy giving information about long range order, local structure and chemical composition.
Background: Secretion of recombinant proteins in yeast can be affected by their improper folding in the endoplasmic reticulum and subsequent elimination of the misfolded molecules via the endoplasmic reticulum associated protein degradation pathway. Recombinant proteins can also be degraded by the vacuolar protease complex. Human urokinase type plasminogen activator (uPA) is poorly secreted by yeast but the mechanisms interfering with its secretion are largely unknown.
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