A Hexameric Ribozyme Nanostructure Formed by Double-Decker Assembly of a Pair of Triangular Ribozyme Trimers

The modular architecture of naturally occurring ribozymes makes them a promising class of structural platform for the design and assembly of three-dimensional (3D) RNA nanostructures, into which the catalytic ability of the platform ribozyme can be installed. We have constructed and analyzed RNA nanostructures with polygonal-shaped (closed) ribozyme oligomers by assembling unit RNAs derived from the Tetrahymena group I intron with a typical modular architecture. In this study, we dimerized ribozyme trimers with a triangular shape by introducing three pillar units. The resulting double-decker nanostructures containing six ribozyme units were characterized biochemically and their structures were observed by atomic force microscopy. The double-decker hexamers exhibited higher catalytic activity than the parent ribozyme trimers.     

Increase of inductance ratio of flat type fault current limiter with high‐Tc superconducting disk

Fault current limiters (FCLs) are expected to reduce fault current and improve stability of power systems. A flat type fault current limiter consisting of the pancake primary winding and a high‐T_c superconducting (HTS) disk was proposed as a modified version of a conventional magnetic shield type of the FCL with the superconducting cylinder. The flat type FCL has the advantage of being manufactured smaller than the cylinder type FCL. It is pointed out, from a magnetic field analysis, that the volume of the flat type FCL is smaller than that of the cylinder type FCL with same magnitude of the limiting inductance. Further, the magnetic field analysis suggests that a high inductance ratio can be realized by radially enlarging both the primary winding and the HTS disk, stacking the FCL modules in layers and sandwiching the primary winding with superconducting disks. © 2006 Institute of Electrical Engineers of Japan. Published by John Wiley & Sons, Inc.     

Evaluation of the contents and ratios of five fractionated proteins to elucidate the protein composition in soybean seeds

Selecting suitable soybean cultivars is important for food processing and exploring their endowment with desirable physiological functions. We applied the fractionation method previously established to compare soy protein composition among cultivars to promote such a selection. More than 95% of the proteins in soybean cotyledons were extracted from 13 soybean cultivars using a high-concentration salt solution. The extracted proteins were fractionated into five fractions, namely oil body-associated protein (OBAP), polar lipid-associated protein (PLAP), globulins (11S and 7S), and whey by centrifugation after tuning the solubility behavior of the proteins with various solutions. Protein species in each fraction were analyzed by SDS-PAGE. Protein content in the total extract and five fractions was quantified to characterize the protein composition of soybean cultivars. The correlation between the protein content of each fraction and the total protein in cotyledon was investigated. A strong positive correlation was found only for the 11S fraction (r = 0.82), followed by a positive correlation in the 7S fraction (r = 0.65). Thus, we surmised that the increased protein content in soybean was due to increased globulin content. Furthermore, the calculation of the average ratio of protein content in each fraction indicated the globulin fraction (7S and 11S) to be 52%, the lipophilic protein fraction (OBAP and PLAP) to be 33%, and the whey fraction to be 13%. The preparation method employed in this study is a promising tool for efficiently comparing the protein composition of soybean cultivars to evaluate the potential use of cultivars for food production.