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Biomedical subjects

W B Whitten

Publications and source records attributed to W B Whitten.

9 recordsLinked to original sources

Microfabricated quadrupole ion trap for mass spectrometer applications.

An array of miniaturized cylindrical quadrupole ion traps, with a radius of 20 microm, is fabricated using silicon micromachining using phosphorus doped polysilicon and silicon dioxide for the purpose of creating a mass spectrometer on a chip. We have operated the array for mass-selective ion ejection and mass analysis using Xe ions at a pressure of 10(-4). The scaling rules for the ion trap in relation to operating pressure, voltage, and frequency are examined.

Journal Article↗

Pulsed-ionization miniature ion mobility spectrometer.

We have demonstrated a miniature ion mobility spectrometer (IMS) that employs single pulses of corona discharge ionization. IMS spectra of both positive and negative ions generated from ambient air were measured as a function of drift field under various ionization conditions. Ion mobility spectra were studied with various pulse widths for both positive and negative ions, giving insights into mechanisms and kinetics of corona discharge ionization used in the miniature IMS. A combination of a pulsed potential with a steady dc bias was used to generate ions in the miniature IMS. There was a threshold dc potential for ion generation for a given pulse height. The dc ionization threshold was found to decrease linearly with increasing pulse height.

Journal Article↗

Space charge effects on resolution in a miniature ion mobility spectrometer.

Miniaturization of ion mobility spectrometry (IMS) is expected to have many advantages, as well as difficulties, in the separation of chemical species at atmospheric pressure. We report the results of studies of a miniature ion mobility spectrometer that has a drift channel 1.7 mm in diameter, the smallest cross section reported to date. The miniature cell contains a homogeneous drift field and is operated at atmospheric pressure. The miniature IMS has been characterized by measuring both negative and positive ion spectra using a frequency-quadrupled Nd: YAG laser on samples of NO, O2, and methyl iodide; a useful resolution (> 10) was achieved with an operating voltage of 500 V. Peak broadening due to Coulomb repulsion was determined to have a major effect on the resolution of the miniature device.

Journal Article↗

Laser desorption/in situ chemical ionization aerosol mass spectrometry for monitoring tributyl phosphate on the surface of environmental particles.

The possibility of using real-time aerosol mass spectrometry (RTAMS) for the detection of surface-adsorbed tributyl phosphate (TBP) as an alkali metal adduct has been investigated. Environmental particles contain variable amounts of easily ionizable alkali metals. During laser desorption of surface-adsorbed TBP molecules, Na+ and K+ ions are generated by the interaction of the laser radiation with the particle's material. The alkali metal ions serve as in situ chemical ionization reagents of the neutral analyte molecules. The effect of laser fluence on the signal intensities of the potassium ion and cationized TBP was also studied. The best performance of the instrument was observed with laser fluences that produce high abundances of K+ but low abundances of ions from the particle's bulk material. The relatively low laser fluence, necessary to produce potassium ions, prevents the excessive fragmentation of the analyte. The instrument is capable of real-time monitoring of submonolayer coverage of TBP on the surface of micron-sized particles.

Organophosphates↗

Laser desorption/ionization coupled to tandem mass spectrometry for real-time monitoring of paraquat on the surface of environmental particles.

Aerosol mass spectrometry with laser desorption/ionization was investigated as a possible tool for real-time monitoring of the presence of the pesticide paraquat on the surface of airborne soil particles. Laser desorption/ionization of paraquat dication produced only singly charged ions. The most abundant species were [M](+.), [M - H](+), and [M - CH3](+). Operation of the ion trap mass spectrometer in the MS(3) mode allowed the reduction of the signal dependence on laser fluence fluctuations and permitted the detection of the analyte with good sensitivity and high selectivity. The estimated limit of detection in terms of surface coverage was 0.016 monolayers, approximately 1 attomole of paraquat on the surface of a single micron-sized soil particle.

Air Pollutants↗

Seven-fold exciton splitting of the 810-nm band in bacteriochlorophyll A-proteins from green photosynthetic bacteria.

We report comparative absorbance and fourth derivative absorbance spectra of two different bacteriochlorophyll a-proteins at 5 K in each of two different cryogenic solvent mixtures. In previous studies at 5 K each protein was observed in only one of these mixtures (not the same one). For the protein from Prosthecochloris aestuarii strain 2K, whose structure is known, the solvent effect is relatively small; for the protein from Chlorobium limicola f. sp. thiosulfatophilum strain 6230 (Tassajara), the effect is much more pronounced. From these results together with earlier results at 300 K, we conclude there may be slight conformational differences of the Prosthecochloris protein between the crystalline form used for X-ray diffraction studies and that in a cryogenic solvent. By comparing spectral features of the two proteins in the same solvent, we are able for the first time to assign all seven of the expected exciton levels in each protein. These occur at 793, 801, 806, 810, 814, 819, and 825 nm in the Prosthecochloris protein, and at 793, 802, 806, 810, 816, 820, and 823 nm in the Chlorobium protein.

Bacteria↗

Linear dichroism of electric field oriented bacteriochlorophyll alpha-protein from green photosynthetic bacteria.

Bacteriochlorophyll alpha-protein from Prosthecochloris aestuarii strain 2K was oriented in a pulsed electric field. The room temperature linear dichroism spectrum of the oriented protein in the Qy region of the bacteriochlorophyll alpha absorption exhibits a single asymmetrical peak at 813 nm with a shoulder extending to the blue. The approximately equal 12 nm fullwidth of the linear dichroism peak is only about half that of the 300 K absorption spectrum. The linear dichroism at 813 nm was not saturated at field strengths of up to 15 kV/cm. The time dependence of the linear dichroism suggests that the orienting particles are aggregates of at least some tens of bacteriochlorophyll alpha-protein trimers. The linear dichroism peak coincides in wavelength with the 813-nm peak of the 300 K, 4th derivative absorption spectrum of the protein and is therefore attributed to the bacteriochlorophyll a Qy exciton transition observed in absorption at the same wavelength.

Bacteria↗

Derivative absorption spectroscopy from 5--300 K of Prosthecochloris aestuarii.

Absorption spectra of the bacteriochlorophyll a-protein from Prosthecochloris aesturaii were measured at temperatures from 2.9 to 300 K. Fourth and eight derivatives of the spectra were calculated from the digital data. From an analysis of 34 scans taken from 750 to 850 nm at 5 K, and 130 scans taken from 822 to 838 nm, we find evidence for nine peaks, six of which are probably 0--0 excitonic and three probably higher vibronic features. The major peaks are resolved in the derivative spectra to 300 K, and all shift with temperature by less than 1 nm compared to their 5 K positions, except for the 825 nm peak which shifts about 2 nm. The most prominent fourth derivative peak at 300 K shifts from 812.9 nm in the standard buffer solution to 814.1 nm in the cryogenic solution in which our low temperature measurements were made. We conclude that the conformation of the protein at 5 K is essentially the same as at 300 K.

Bacteria↗