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This paper introduces a tool for the optimization of CMOS integrated spiral inductors. Its aim is to offer designers a first approach on designing inductors without the need for fabrication. The core of the tool is an optimization procedure where technology constraints on the inductor layout parameters are considered by applying user-defined discretization on the design variables. User-defined constraints between layout parameters may also be accounted for, as a way of taking into account design heuristics. For those cases where the device area is a major concern area minimization may be considered. On the other hand, if a major design goal is the inductor quality factor the tool may yield the layout parameters which maximize the quality factor. The trade-off between quality factor and device area is evaluated through the generation of a graphical representation of quality factor versus output diameter for a given inductance. For the sake of simplicity the pi-model has been used for characterising the inductor. The application was developed in Matlab and the optimization toolbox is used. The validity of the design results obtained is checked against circuit simulation with ASITIC.

Nitric Oxide Reductase (NOR) is an integral membrane protein performing the reduction of NO to N(2)O. NOR is composed of two subunits: the large one (NorB) is a bundle of 12 transmembrane helices (TMH). It contains a b type heme and a binuclear iron site, which is believed to be the catalytic site, comprising a heme b and a non-hemic iron. The small subunit (NorC) harbors a cytochrome c and is attached to the membrane through a unique TMH. With the aim to perform structural and functional studies of NOR, we have immunized dromedaries with NOR and produced several antibody fragments of the heavy chain (VHHs, also known as nanobodies (TM)). These fragments have been used to develop a faster NOR purification procedure, to proceed to crystallization assays and to analyze the electron transfer of electron donors. BIAcore experiments have revealed that up to three VHHs can bind concomitantly to NOR with affinities in the nanomolar range. This is the first example of the use of VHHs with an integral membrane protein. Our results indicate that VHHs are able to recognize with high affinity distinct epitopes on this class of proteins, and can be used as versatile and valuable tool for purification, functional study and crystallization of integral membrane proteins.

Copper oxide thin films were obtained by annealing (temperature ranging between 100 and 450 °C) the metallic Cu films deposited on glass substrates by e-beam evaporation. XRD studies confirmed that the cubic Cu phase of the asdeposited films changes into single cubic Cu 2Ophase and single monoclinic CuO phase, depending on the annealing conditions. The crystallite size is varied betweeñ12 and 31 nm. The lattice parameters of cubic Cu and Cu 2Ophases are estimated tõ3.60 and ̃4.26 Å , respectively. The films with Cu 2O phase showed p-type characteristics. The conductivity is decreased linearly with the decreasing temperature (1/T), which has confirmed the semiconductor nature of the deposited films. The calculated activation energy is varied between 0.10 and 0.16 eV. The surface microstructure is changed depending on the variation in the annealing temperature. The poor transmittance of the asdeposited films (<1%) is increased to a maximum of ̃80% (800 nm) on annealing at 200 °C. The estimated direct allowed band gap is varied between 1.73 and 2.89 eV. © 2009 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.