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We put forward nonadiabatic charge pumping as a method for accessing the different charge relaxation rates as well as the relaxation rates of excited orbital states in double-quantum-dot setups, based on extremely size-limited quantum dots and dopant systems. The rates are obtained in a well-separated manner from plateaus, occurring when comparing the steady-state current for reversed driving cycles. This yields a reliable readout independent of any fitting parameters. Importantly, the nonadiabatic pumping spectroscopy essentially exploits the same driving scheme as the operation of these devices generally employs. We provide a detailed analysis of the working principle of the readout scheme as well as of possible errors, thereby demonstrating its broad applicability. The precise knowledge of relaxation rates is highly relevant for the implementation of time-dependently operated devices, such as electron pumps for metrology or qubits in quantum information., Comment: 14 pages, 5 figures

We present a systematic study of various ways (top gates, local doping, substrate bias) to fabricate and tune multi-dot structures in silicon nanowire multigate MOSFETs (metal-oxide-semiconductor field-effect transistors). The carrier concentration profile of the silicon nanowire is a key parameter to control the formation of tunnel barriers and single-electron islands. It is determined both by the doping profile of the nanowire and by the voltages applied to the top gates and to the substrate. Local doping is achieved with the realisation of up to two arsenic implantation steps in combination with gates and nitride spacers acting as a mask. We compare nominally identical devices with different implantations and different voltages applied to the substrate, leading to the realisation of both intrinsic and doped coupled dot structures. We demonstrate devices in which all the tunnel resistances towards the electrodes and between the dots can be independently tuned with the control top gates wrapping the silicon nanowire., 7 pages, 6 figures

As in eukaryotes, phosphorylation of Ser and Thr residues in proteins appears to be a common phenomenon in bacteria. Surprisingly, however, very few Ser/Thr protein kinases have been identified and in this study antibodies directed against mammalian protein kinase C (PKC) have been used in attempts to isolate conserved Ser/Thr protein kinases. Using the mAb M7 against rat brain PKC, a single 70 kDa band was identified in total cell extracts of Bacillus subtilis by Western blotting after SDS-PAGE, whilst using polyclonal antibody α-PKC1p against Saccharomyces cerevisiae PKC a single 67 kDa band was identified by the same procedure. The two proteins were purified independently on the basis of antibody recognition employing two-dimensional gel electrophoresis as a final step, which allowed subsequent microsequencing. The 70 kDa band was thus identified as the phosphoenolpyruvate-dependent His HPr kinase, Enzyme I of the phosphotransferase system. This identity was confirmed using a mutant deleted for ptsl, encoding Enzyme I. The 67 kDa protein was identified as a previously unknown B. subtilis ‘trigger factor’, homologous to an Escherichia coli protein-folding enzyme, peptidylprolyl cis-trans-isomerase implicated in cell division.