Arctic and subarctic environmental analyses utilizing ERTS-1 imagery

The author has identified the following significant results. ERTS-1 imagery provides a means of distinguishing and monitoring estuarine surface water circulation patterns and changes in the relative sediment load of discharging rivers on a regional basis. Physical boundaries mapped from ERTS-1 imagery in combination with ground truth obtained from existing small scale maps and other sources resulted in improved and more detailed maps of permafrost terrain and vegetation for the same area. Snowpack cover within a research watershed has been analyzed and compared to ground data. Large river icings along the proposed Alaska pipeline route from Prudhoe Bay to the Brooks Range have been monitored. Sea ice deformation and drift northeast of Point Barrow, Alaska have been measured during a four day period in March and shore-fast ice accumulation and ablation along the west coast of Alaska have been mapped for the spring and early summer seasons

Probing the Reaction Mechanism of the D-ala-D-ala Dipeptidase, VanX, by Using Stopped-Flow Kinetic and Rapid-Freeze Quench EPR Studies on the Co(II)-Substituted Enzyme

In an effort to probe the reaction mechanism of VanX, the D-ala-D-ala dipeptidase required for high-level vancomycin resistance in bacteria, stopped-flow kinetic and rapid-freeze quench EPR studies were conducted on the Co(II)-substituted enzyme when reacted with d-ala-d-ala. The intensity of the Co(II) ligand field band at 550 nm decreased (ε550 = 140 to 18 M-1 cm-1) when VanX was reacted with substrate, suggesting that the coordination number of the metal increases from 5 to 6 upon substrate binding. The stopped-flow trace was fitted to a kinetic mechanism that suggests the presence of an intermediate whose breakdown is rate-limiting. Rapid-freeze quench EPR studies verified the presence of a reaction intermediate that exhibits an unusually low hyperfine constant (33 G), which suggests a bidentate coordination of the intermediate to the metal center. The EPR studies also identified a distinct enzyme product complex. The results were used to offer a detailed reaction mechanism for VanX that can be used to guide future inhibitor design efforts

College students’ perceptions regarding sensory aspects of conventionally produced and unconventionally produced foods: implications for marketing to the Millennial generation

Consumers vote every day on which products line the shelves of grocery stores, co-ops, and niche markets. Public unrest with regard to the environmental, animal welfare, food purity, and human health impacts of agricultural production practices have led to the rise of unconventionally produced (UP) food products. While the sales of UP foods is increasing, studies regarding the qualities of such products that impact consumer purchases have yielded inconsistent results. This study examined students’ perceptions of sensory aspects of conventionally produced (CP) and UP foods to better understand how sensory aspects impact decisions to purchase. Students reported consistent perceptions regarding the favorability of each sensory aspect of chicken and apples; the UP versions of the products yielded higher mean scores on every sensory aspect. However, students’ perceptions of the sensory qualities of chocolate, milk, and beef were not consistent; for example, they reported more favorable perceptions of the appearance and smell of CP milk, but perceived a more favorable texture and flavor from the UP milk. The results of this study imply that when making purchasing decisions, consumers may value specific sensory attributes over others. One approach to marketing UP products is to focus on valued extrinsic aspects designed to attract consumers to purchase products even though they may have less favorable perceptions of certain sensory qualities

College Students\u27 Perceptions regarding Sensory Aspects of Conventionally Produced and Unconventionally Produced Foods: Implications for Marketing to the Millennial Generation

Every day consumers vote which products line the shelves of grocery stores, co-ops, and niche markets by use of their dollars. Public unrest with regard to the environment, animal welfare, food purity, and human health impacts of agricultural production practices have led to the rise of alternatively produced food products. While the sales of alternatively produced foods are increasing, studies regarding the qualities of such products impact consumer purchases have yielded inconsistent results. This study examined students’ perceptions of sensory aspects of conventionally produced and alternatively produced foods to better understand how sensory aspects impact decisions to purchase. Students reported consistent perceptions regarding the favorability of each sensory aspect of chicken and apples; the alternatively produced versions of the products yielded higher mean scores on every sensory aspect. However, students’ perceptions of the sensory qualities of chocolate, milk, and beef were not consistent; for example, they reported more favorable perceptions of the appearance and smell of conventionally produced milk, but perceived a more favorable texture and flavor from the alternatively produced milk. The results of this study imply when making purchasing decisions, consumers may value specific sensory attributes over others. An alternative approach to marketing alternatively produced products is to focus on valued extrinsic aspects designed to attract consumers to purchase products in spite of their perhaps less valued perceptions of sensory aspects

Structural Studies on a Mitochondrial Glyoxalase II

Glyoxalase 2 is a β-lactamase fold-containing enzyme that appears to be involved with cellular chemical detoxification. Although the cytoplasmic isozyme has been characterized from several organisms, essentially nothing is known about the mitochondrial proteins. As a first step in understanding the structure and function of mitochondrial glyoxalase 2 enzymes, a mitochondrial isozyme (GLX2-5) from Arabidopsis thaliana was cloned, overexpressed, purified, and characterized using metal analyses, EPR and 1H NMR spectroscopies, and x-ray crystallography. The recombinant enzyme was shown to bind 1.04 ± 0.15 eq of iron and 1.31 ± 0.05 eq of Zn(II) and to exhibit kcat and Km values of 129 ± 10 s-1 and 391 ± 48 μm, respectively, when using S-d-lactoylglutathione as the substrate. EPR spectra revealed that recombinant GLX2-5 contains multiple metal centers, including a predominant Fe(III)Z-n(II) center and an anti-ferromagnetically coupled Fe(III)Fe(II) center. Unlike cytosolic glyoxalase 2 from A. thaliana, GLX2-5 does not appear to specifically bind manganese. 1H NMR spectra revealed the presence of at least eight paramagnetically shifted resonances that arise from protons in close proximity to a Fe(III)Fe(II) center. Five of these resonances arose from solvent-exchangeable protons, and four of these have been assigned to NH protons on metal-bound histidines. A 1.74-Å resolution crystal structure of the enzyme revealed that although GLX2-5 shares a number of structural features with human GLX2, several important differences exist. These data demonstrate that mitochondrial glyoxalase 2 can accommodate a number of different metal centers and that the predominant metal center is Fe(III)Zn(II)

A Five-coordinate Metal Center in Co(II)-substituted VanX

In an effort to structurally probe the metal binding site in VanX, electronic absorption, EPR, and extended x-ray absorption fine structure (EXAFS) spectroscopic studies were conducted on Co(II)-substituted VanX. Electronic spectroscopy revealed the presence of Co(II) ligand field transitions that had molar absorptivities of ∼100 m–1 cm–1, which suggests that Co(II) is five-coordinate in Co(II)-substituted VanX. Low temperature EPR spectra of Co(II)-substituted VanX were simulated using spin Hamiltonian parameters of M = |±½〉, E/D = 0.14, greal(x,y) = 2.37, and grealS(z) = 2.03. These parameters lead to the prediction that Co(II) in the enzyme is five-coordinate and that there may be at least one solvent-derived ligand. Single scattering fits of EXAFS data indicate that the metal ions in both native Zn(II)-containing and Co(II)-substituted VanX have the same coordination number and that the metal ions are coordinated by 5 nitrogen/oxygen ligands at ∼ 2.0 Å. These data demonstrate that Co(II) (and Zn(II) from EXAFS studies) is five-coordinate in VanX in contrast to previous crystallographic studies (Bussiere, D. E., Pratt, S. D., Katz, L., Severin, J. M., Holzman, T., and Park, C. H. (1998) Mol. Cell 2, 75–84). These spectroscopic studies also demonstrate that the metal ion in Co(II)-substituted VanX when complexed with a phosphinate analog of substrate d-Ala-d-Ala is also five-coordinate

Glyoxalase II from A. thaliana requires Zn(II) for catalytic activity

AbstractCytosolic glyoxalase II from Arabidopsis thaliana, GLX2-2, was overexpressed and purified to homogeneity using Q-sepharose chromatography. MALDI-TOF mass spectrometry studies indicated a molecular weight of 28 767 Da. Using steady-state kinetics studies, the purified enzyme exhibited a Km of 660±100 μM and a kcat of 484±92 s−1 at 37°C. Metal analyses demonstrated that the enzyme binds 2.1±0.5 moles of Zn(II) per monomer; the binding of Zn(II) is essential for enzyme viability and activity. Sequence comparison of glyoxalase II enzymes from human, A. thaliana, and yeast and the metallo-β-lactamases reveal that all metal binding ligands of the metallo-β-lactamases are conserved in glyoxalase II enzymes, suggesting that all glyoxalase II enzymes are Zn(II) metalloenzymes. These results and their implications are discussed in light of previous studies on glyoxalase II, and an active site for the glyoxalase II enzymes is proposed

LISA Data Analysis using MCMC methods

The Laser Interferometer Space Antenna (LISA) is expected to simultaneously detect many thousands of low frequency gravitational wave signals. This presents a data analysis challenge that is very different to the one encountered in ground based gravitational wave astronomy. LISA data analysis requires the identification of individual signals from a data stream containing an unknown number of overlapping signals. Because of the signal overlaps, a global fit to all the signals has to be performed in order to avoid biasing the solution. However, performing such a global fit requires the exploration of an enormous parameter space with a dimension upwards of 50,000. Markov Chain Monte Carlo (MCMC) methods offer a very promising solution to the LISA data analysis problem. MCMC algorithms are able to efficiently explore large parameter spaces, simultaneously providing parameter estimates, error analyses and even model selection. Here we present the first application of MCMC methods to simulated LISA data and demonstrate the great potential of the MCMC approach. Our implementation uses a generalized F-statistic to evaluate the likelihoods, and simulated annealing to speed convergence of the Markov chains. As a final step we super-cool the chains to extract maximum likelihood estimates, and estimates of the Bayes factors for competing models. We find that the MCMC approach is able to correctly identify the number of signals present, extract the source parameters, and return error estimates consistent with Fisher information matrix predictions.Comment: 14 pages, 7 figure

Sensitivity and parameter-estimation precision for alternate LISA configurations

We describe a simple framework to assess the LISA scientific performance (more specifically, its sensitivity and expected parameter-estimation precision for prescribed gravitational-wave signals) under the assumption of failure of one or two inter-spacecraft laser measurements (links) and of one to four intra-spacecraft laser measurements. We apply the framework to the simple case of measuring the LISA sensitivity to monochromatic circular binaries, and the LISA parameter-estimation precision for the gravitational-wave polarization angle of these systems. Compared to the six-link baseline configuration, the five-link case is characterized by a small loss in signal-to-noise ratio (SNR) in the high-frequency section of the LISA band; the four-link case shows a reduction by a factor of sqrt(2) at low frequencies, and by up to ~2 at high frequencies. The uncertainty in the estimate of polarization, as computed in the Fisher-matrix formalism, also worsens when moving from six to five, and then to four links: this can be explained by the reduced SNR available in those configurations (except for observations shorter than three months, where five and six links do better than four even with the same SNR). In addition, we prove (for generic signals) that the SNR and Fisher matrix are invariant with respect to the choice of a basis of TDI observables; rather, they depend only on which inter-spacecraft and intra-spacecraft measurements are available.Comment: 17 pages, 4 EPS figures, IOP style, corrected CQG versio

Dilution of Dipolar Interactions in a Spin-labeled, Multimeric Metalloenzyme for DEER Studies

The metallo-β-lactamases (MβLs), which require one or two Zn(II) ions in their active sites for activity, hydrolyze the amide bond in β-lactam-containing antibiotics, and render the antibiotics inactive. All known MβLs contain a mobile element near their active sites, and these mobile elements have been implicated in the catalytic mechanisms of these enzymes. However little is known about the dynamics of these elements. In this study, we prepared a site-specific, double spin-labeled analog of homotetrameric MβL L1 with spin labels at positions 163 and 286 and analyzed the sample with DEER (double electron electron resonance) spectroscopy. Four unique distances were observed in the DEER distance distribution, and these distances were assigned to the desired intramolecular dipolar coupling (between spin labels at positions 163 and 286 in one subunit) and to intermolecular dipolar couplings. To rid the spin-labeled analog of L1 of the intermolecular couplings, spin-labeled L1 was “diluted” by unfolding/refolding the spin-labeled enzyme in the presence of excess wild-type L1. DEER spectra of the resulting, spin-diluted enzyme revealed a single distance corresponding to the desire intramolecular dipolar coupling