Upgrade of the DIII-D RF systems

The DIII-D Advanced Tokamak Program requires the ability to modify the current density profile for extended time periods in order to achieve the improved plasma conditions now achieved with transient means. To support this requirement DIII-D has just completed a major addition to its ion cyclotron range of frequency (ICRF) systems. This upgrade project added two new fast wave current drive (FWCD) systems, with each system consisting of a 2 MW, 30 to 120 MHz transmitter, an all ceramic insulated transmission line, and water-cooled four-strap antenna. With this addition of 4 MW of FWCD power to the original 2 MW, 30 to 60 MHz capability, experiments can be performed with centrally localized current drive enhancement. For off-axis current modification, plans are in place to add 110 GHz electron cyclotron heating (ECH) power to DIII-D. Initially, 3 MW of power will be available with plans to increase the power to 6 MW and to 10 MW

4 MW Fast Wave Current Drive Upgrade for DIII-D

The DIII-D program has just completed a major addition to its ion cyclotron range of frequency (ICRF) systems. This upgrade project added two new fast wave current drive (FWCD) systems, with each system consisting of a 2 MW, 30 to 120 MHz transmitter, ceramic insulated transmission lines and tuner elements, and water-cooled four-strap antenna. With this addition of 4 MW of FWCD power to the original 2 MW, 30 to 60 MHz capability, experiments can be performed that will explore advanced tokamak plasma configurations by using the centrally localized current drive to effect current profile modifications

Structure of the Cytoplasmic Loop between Putative Helices II and III of the Mannitol Permease of Escherichia coli: A Tryptophan and 5-Fluorotryptophan Spectroscopy Study

In this work, four single tryptophan (Trp) mutants of the dimeric mannitol transporter of Escherichia coli, EIImtl, are characterized using Trp and 5-fluoroTrp (5-FTrp) fluorescence spectroscopy. The four positions, 97, 114, 126, and 133, are located in a region shown by recent studies to be involved in the mannitol translocation process. To spectroscopically distinguish between the Trp positions in each subunit of dimeric EIImtl, 5-FTrp was biosynthetically incorporated because of its much simpler photophysics compared to those of Trp. The steady-state and time-resolved fluorescence methodologies used point out that all four positions are in structured environments, both in the absence and in the presence of a saturating concentration of mannitol. The fluorescence decay of all 5-FTrp-containing mutants was highly homogeneous, suggesting similar microenvironments for both probes per dimer. However, Stern-Volmer quenching experiments using potassium iodide indicate different solvent accessibilities for the two probes at positions 97 and 133. A 5 Å two-dimensional (2D) projection map of the membrane-embedded IICmtl dimer showing 2-fold symmetry is available. The results of this work are in better agreement with a 7 Å projection map from a single 2D crystal on which no symmetry was imposed.

Effect of cyclosporin A on proteinuria in the course of glomerulopathy associated with WT1 mutations

Denys–Drash syndrome (DDS) is characterized by progressive glomerulopathy caused by diffuse mesangial sclerosis (DMS), genitourinary defects, and a higher risk of developing Wilms’ tumor. It is commonly assumed that the DMS is unresponsive to any medications. In this report, we present a patient with Denys–Drash syndrome, in whom the cyclosporine A (CsA) was found to induce total remission. This observation and observations of other authors confirm that in genetic forms of nephrotic syndrome, the proteinuric effect of CsA may be due to a non-immunologic mechanism. We confirm the beneficial effect of CsA treatment in DDS; however, the potential nephrotoxicity of this drug will probably not allow long-term use

Recent developments on the high power ECH installation at the DIII-D tokamak

The 110 GHz gyrotron installation on the DIII-D tokamak has been upgraded to three tubes in the megawatt class with plans for further upgrades. The latest addition uses a diamond output window. The report describes the installation, plans, and experimental results to date

RF power diagnostics and control on the DIII-D, 4 MW 30--120 MHz fast wave current drive system (FWCD)

The Fast Wave Current Drive System uses three 2 MW transmitters to drive three antennas inside the DIII-D vacuum vessel. This paper describes the diagnostics for this system. The diagnostics associated with the General Atomics Fast Wave Current Drive System allow the system tuning to be analyzed and modified on a between shot basis. The transmitters can be exactly tuned to match the plasma with only one tuning shot into the plasma. This facilitates maximum rf power utilization

Mechanism of the Very Efficient Quenching of Tryptophan Fluorescence in Human γD- and γS-Crystallins: The γ-Crystallin Fold May Have Evolved To Protect Tryptophan Residues from Ultraviolet Photodamage†

Proteins exposed to UV radiation are subject to irreversible photodamage through covalent modification of tryptophans (Trps) and other UV-absorbing amino acids. Crystallins, the major protein components of the vertebrate eye lens that maintain lens transparency, are exposed to ambient UV radiation throughout life. The duplicated β-sheet Greek key domains of β- and γ-crystallins in humans and all other vertebrates each have two conserved buried Trps. Experiments and computation showed that the fluorescence of these Trps in human γD-crystallin is very efficiently quenched in the native state by electrostatically enabled electron transfer to a backbone amide [Chen et al. (2006) Biochemistry 45, 11552−11563]. This dispersal of the excited state energy would be expected to minimize protein damage from covalent scission of the excited Trp ring. We report here both experiments and computation showing that the same fast electron transfer mechanism is operating in a different crystallin, human γS-crystallin. Examination of solved structures of other crystallins reveals that the Trp conformation, as well as favorably oriented bound waters, and the proximity of the backbone carbonyl oxygen of the n − 3 residues before the quenched Trps (residue n), are conserved in most crystallins. These results indicate that fast charge transfer quenching is an evolved property of this protein fold, probably protecting it from UV-induced photodamage. This UV resistance may have contributed to the selection of the Greek key fold as the major lens protein in all vertebrates.National Eye Institute (Grant EY 015834