Tests for conceptual design of 6.6 kV class superconducting fault current limiter with YBCO thin film elements

A superconducting fault current limiter (SFCL) for 6.6 kV and 400 A installed in a cubicle for a distribution network substation was conceptually designed. The SFCL consists of parallel- and series-connected superconducting YBCO elements and a limiting resistor. Before designing the SFCL, some tests were carried out. The width and length of each element used in the tests are 30 mm and 210 mm, respectively. The element consists of YBCO thin film of about 200 nm in thickness on cerium dioxide (CeO2) as a cap-layer on a sapphire substrate by metal-organic deposition with a protective metal coat. In the tests, characteristics of each element, such as over-current, withstand-voltage, and so on, were obtained. From these characteristics, series and parallel connections of the elements, called units, were considered. The characteristics of the units were obtained by tests. From the test results, a single phase prototype SFCL was manufactured and tested. Thus, an SFCL rated at 6.6 kV and 400 A can be designed. © 2009 IEEE.

Surface attachment of protein fibrils via covalent modification strategies.

Chemical control of surface functionality and topography is an essential requirement for many technological purposes. In particular, the covalent attachment of monomeric proteins to surfaces has been the object of intense studies in recent years, for applications as varied as electrochemistry, immuno-sensing, and the production of biocompatible coatings. Little is known, however, about the characteristics and requirements underlying surface attachment of supramolecular protein nanostructures. Amyloid fibrils formed by the self-assembly of peptide and protein molecules represent one important class of such structures. These highly organized beta-sheet-rich assemblies are a hallmark of a range of neurodegenerative disorders, including Alzheimer's disease and type II diabetes, but recent findings suggest that they have much broader significance, potentially representing the global free energy minima of the energy landscapes of proteins and having potential applications in material science. In this paper, we describe strategies for attaching amyloid fibrils formed from different proteins to gold surfaces under different solution conditions. Our methods involve the reaction of sulfur containing small molecules (cystamine and 2-iminothiolane) with the amyloid fibrils, enabling their covalent linkage to gold surfaces. We demonstrate that irreversible attachment using these approaches makes possible quantitative analysis of experiments using biosensor techniques, such as quartz crystal microbalance (QCM) assays that are revolutionizing our understanding of the mechanisms of amyloid growth and the factors that determine its kinetic behavior. Moreover, our results shed light on the nature and relative importance of covalent versus noncovalent forces acting on protein superstructures at metal surfaces.