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Energy transport in short-pulse-laser-heated targets measured using extreme ultraviolet laser backlighting.
Phys Rev E Stat Nonlin Soft Matter Phys
August 2012
York Plasma Institute, The Department of Physics, The University of York, York, UK.
The accurate characterization of thermal electron transport and the determination of heating by suprathermal electrons in laser driven solid targets are both issues of great importance to the current experiments being performed at the National Ignition Facility, which aims to achieve thermonuclear fusion ignition using lasers. Ionization, induced by electronic heat conduction, can cause the opacity of a material to drop significantly once bound-free photoionization is no longer energetically possible. We show that this drop in opacity enables measurements of the transmission of extreme ultraviolet (EUV) laser pulses at 13.
View Article and Find Full Text PDFExtreme ultraviolet interferometry of warm dense matter in laser plasmas.
Opt Lett
November 2010
Department of Physics, University of York, York YO10 5DD, UK.
We demonstrate that interferometric probing with extreme ultraviolet (EUV) laser light enables determination of the degree of ionization of the "warm dense matter" produced between the critical and ablation surfaces of laser plasmas. Interferometry has been utilized to measure both transmission and phase information for an EUV laser beam at the photon energy of 58.5 eV, probing longitudinally through laser-irradiated plastic (parylene-N) targets (thickness 350 nm) irradiated by a 300 ps duration pulse of wavelength 438 nm and peak irradiance 10(12) W cm(-2).
View Article and Find Full Text PDFLaser spectroscopy of CdKr molecules in ultraviolet region.
Spectrochim Acta A Mol Biomol Spectrosc
October 2002
Instytut Fizyki, Uniwersytet Jagielloński, Kraków, Poland.
Excitation spectra of the A0+(5(3)P1)<--X0+(5(1)S0), B1(5(3)P1)<--X0+ and D1(5(1)P1)<--X0+ transitions as well as a fluorescence spectrum of the D1(v') = 16 --> X0+ transition in CdKr van der Waals molecule has been recorded in an experiment of a continuous supersonic molecular beam crossed with a pulsed dye laser beam. A rigorous analysis of the excitation spectra based on Birge-Sponer and LeRoy-Bernstein methods aided with a computer calculation, utilizing a program of near dissociation expansion lead to the X0+- and improved A0+-, B1- and D1-state characterizations. Evidence of a theoretically predicted potential barrier within the B1-state well was found and discussed with regard to the latest result of ab initio calculation.
View Article and Find Full Text PDFMolecularly imprinted fluorescent-shift receptors prepared with 2-(trifluoromethyl)acrylic acid.
Anal Chem
July 2000
Laboratory of Synthetic Biochemistry, Faculty of Information Sciences, Hiroshima City University, Japan.
Methacrylic acid (MAA) and 2-(trifluoromethyl)acrylic acid (TFMAA) were used to prepare molecularly imprinted polymers exhibiting diastereoselectivity for cinchona alkaloids. Fluorescent spectra of the cinchona alkaloid exhibit a characteristic shift through binding to these polymer particles, originating most likely from the highly acidic residues in the imprinted polymers acting as a proton donator. Our results show that TFMAA based imprinted polymers can be used as polymer reagents for quantitating the cinchona alkaloid bound to the polymers without bound/free separation.
View Article and Find Full Text PDFStereoselective, competitive, and nonlinear plasma protein binding of ibuprofen enantiomers as determined in vivo in healthy subjects.
J Pharmacokinet Biopharm
April 1993
College of Pharmacy, University of Michigan, Ann Arbor 48109-1065.
The plasma protein binding and competitive inhibition parameters of R(-)- and S(+)-ibuprofen were determined in vivo in 12 healthy subjects. Subjects participated in a 4 x 4 Latin square design in which oral solutions of drug were administered as 300 mg R(-)-ibuprofen, 300 mg S(+)-ibuprofen, 300 mg R(-)- + 300 mg S(+)-ibuprofen, and 300 mg R(-)- + 600 mg S(+)-ibuprofen. Unlabeled ibuprofen enantiomers were quantitated using a stereospecific reversed-phase HPLC assay, and plasma protein binding experiments were performed using radiolabeled 14C-enantiomers and an ultrafiltration method at 37C.
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