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    Single-electron transitions in one-dimensional native nanostructures
    (Bristol : Institute of Physics Publishing, 2014) Reiche, M.; Kittler, M.; Schmelz, M.; Stolz, R.; Pippel, E.; Uebensee, H.; Kermann, M.; Ortlepp, T.
    Low-temperature measurements proved the existence of a two-dimensional electron gas at defined dislocation arrays in silicon. As a consequence, single-electron transitions (Coulomb blockades) are observed. It is shown that the high strain at dislocation cores modifies the band structure and results in the formation of quantum wells along dislocation lines. This causes quantization of energy levels inducing the formation of Coulomb blockades.
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    Process flow to integrate nanostructures on silicon grass in surface micromachined systems
    (Bristol : IOP Publ., 2016) Mehner, H.; Müller, L.; Biermann, S.; Hänschke, F.; Hoffmann, M.
    The process flow to integrate metallic nanostructures in surface micromachining processes is presented. The nanostructures are generated by evaporation of microstructured silicon grass with metal. The process flow is based on the lift-off of a thin amorphous silicon layer deposited using a CVD process. All steps feature a low temperature load beneath 120 °C and high compatibility with many materials as only well-established chemicals are used. As a result metallic nanostructures usable for optical applications can be generated as part of multilayered microsystems fabricated in surface micromachining.
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    High resolution spectroscopy reveals fibrillation inhibition pathways of insulin
    ([London] : Macmillan Publishers Limited, part of Springer Nature, 2016) Deckert-Gaudig, Tanja; Deckert, Volker
    Fibril formation implies the conversion of a protein’s native secondary structure and is associated with several neurodegenerative diseases. A better understanding of fibrillation inhibition and fibril dissection requires nanoscale molecular characterization of amyloid structures involved. Tip-enhanced Raman scattering (TERS) has already been used to chemically analyze amyloid fibrils on a sub-protein unit basis. Here, TERS in combination with atomic force microscopy (AFM), and conventional Raman spectroscopy characterizes insulin assemblies generated during inhibition and dissection experiments in the presence of benzonitrile, dimethylsulfoxide, quercetin, and β-carotene. The AFM topography indicates formation of filamentous or bead-like insulin self-assemblies. Information on the secondary structure of bulk samples and of single aggregates is obtained from standard Raman and TERS measurements. In particular the high spatial resolution of TERS reveals the surface conformations associated with the specific agents. The insulin aggregates formed under different inhibition and dissection conditions can show a similar morphology but differ in their β-sheet structure content. This suggests different aggregation pathways where the prevention of the β-sheet stacking of the peptide chains plays a major role. The presented approach is not limited to amyloid-related reasearch but can be readily applied to systems requiring extremely surface-sensitive characterization without the need of labels.