A DC-powered Josephson logic family that uses hybrid unlatchingflip-flop logic elements (Huffles)

This paper describes the development of a dc-powered Josephson logic family that uses hybrid unlatching flip-flop logic elements (Huffles). The Huffle circuit used in this study is modified by adding a parallel resistor to the original Hebard-type Huffle circuit. Analysis of the circuit's operation shows that the undesirable hung-up phenomena are prevented by this modification. Based on the result of the analysis, the circuit's parameters are derived and a typical operating margin of ±26% is obtained. Besides AND/OR operations using a threshold logic operation, two-input exclusive OR (XOR), two-input multiplexor (MUX), and three-input majority (MAJ) operations are realized using a Huffle gate in which 2-Josephson-interferometers (2JI) in the standard Huffle gate are replaced by stacked-2JI's. Thus, a Huffle logic family, formed from NOT, AND, OR, XOR, MUX, MAJ, and flip-flop (FF), are constructed. By using this Huffle logic family, a 6-b arithmetic logic operating unit (ALU), a 6-b analog-to-digital converter (ADC), and a 6-b gray-to-binary converter (GBC) have been successfully operated. During high-speed testing, a 1-b comparator was operated up to an input bandwidth of 6 GHz     

In vitro selection of proteins that undergo covalent labeling with small molecules by thiol-disulfide exchange by using ribosome display

There is a great deal of interest in proteins that can bind covalently to target molecules, as they allow unambiguous experiments by tight binding to molecules of interest. Here, we report the generation of proteins that undergo covalent labeling with small molecules through in vitro selection by using ribosome display. Selection was performed from a mutant library of the WW domain with a biotinylated peptide as its binding target, in which the biotin and the peptide are connected by a disulfide bond. After five rounds of selection, we identified mutants carrying a particular cysteine mutation. The binding target reacted specifically with the selected mutant, even in the presence of other proteins, and resulted in the generation of biotin- or peptide-labeled WW domains by thiol-disulfide exchange. When the mutant was fused to a protein of interest, the fusion protein was also labeled with biotin. Thus, the characteristics of the selected mutant should be suitable as a tag sequence that can be covalently labeled with small synthetic molecules. These results indicate that the rapid and efficient generation of such proteins is possible by ribosome display.     

Fabrication of fluorine-terminated diamond-like carbon thin film using a hyperthermal atomic fluorine beam

Surface modification of diamond-like carbon (DLC) film was performed using a hyperthermal atomic fluorine beam on the purpose of production of hydrophobic surface by maintaining the high hardness of DLC film. By the irradiation of atomic fluorine beam of a 1.0 × 10²⁰ atoms/cm², the contact angle of a water drop against the DLC surface increased from 73° to 111°. The formation of CF₃, CF₂ and CF bonding on the modified DLC surface was confirmed from the measurements of X-ray photoelectron spectra and near-edge X-ray absorption fine structure spectra. Irradiation of hyperthermal atomic fluorine beam was concluded to produce insulator fluorine-terminated DLC film, which has high F content on the surface, by the taking of the use of neutral atomic beam as a fluorine source.