24 research outputs found

    Airport surface operations requirements analysis

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    This report documents the results of the Airport Surface Operations Requirements Analysis (ASORA) study. This study was conducted in response to task 24 of NASA Contract NAS1-18027. This study is part of NASA LaRC's Low Visibility Surface Operations program, which is designed to eliminate the constraints on all-weather arrival/departure operations due to the airport/aircraft ground system. The goal of this program is to provide the capability for safe and efficient aircraft operations on the airport surface during low visibility conditions down to zero. The ASORA study objectives were to (1) develop requirements for operation on the airport surface in visibilities down to zero; (2) survey and evaluate likely technologies; (3) develop candidate concepts to meet the requirements; and (4) select the most suitable concept based on cost/benefit factors

    Whose knowledge, whose voices? Power, agency and resistance in disability studies for the global south

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    Meekosha (2011) maintains that research and theories about disability derive mainly from the global North. Disability Studies rarely include non-metropolitan thinkers. Even when they do, these studies tend to be seen as context specific, and the social theories which emanate from these studies are rarely refered to in research theorizing disability in the North. This chapter sets out to investigate how this one way transfer of knowledge affects the way Disability Studies is conceptualised - whose experiences are incorporated within these studies; and whose are left out. Multilateral debate and dialogue between Disability Studies academics and activists in different locations around the world would help add on to the knowledge already available in the field, while keeping others informed about what is taking place in 'similar' situations elsewhere.peer-reviewe

    Estimating Contact Process Saturation in Sylvatic Transmission of Trypanosoma cruzi in the United States

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    Although it has been known for nearly a century that strains of Trypanosoma cruzi, the etiological agent for Chagas' disease, are enzootic in the southern U.S., much remains unknown about the dynamics of its transmission in the sylvatic cycles that maintain it, including the relative importance of different transmission routes. Mathematical models can fill in gaps where field and lab data are difficult to collect, but they need as inputs the values of certain key demographic and epidemiological quantities which parametrize the models. In particular, they determine whether saturation occurs in the contact processes that communicate the infection between the two populations. Concentrating on raccoons, opossums, and woodrats as hosts in Texas and the southeastern U.S., and the vectors Triatoma sanguisuga and Triatoma gerstaeckeri, we use an exhaustive literature review to derive estimates for fundamental parameters, and use simple mathematical models to illustrate a method for estimating infection rates indirectly based on prevalence data. Results are used to draw conclusions about saturation and which population density drives each of the two contact-based infection processes (stercorarian/bloodborne and oral). Analysis suggests that the vector feeding process associated with stercorarian transmission to hosts and bloodborne transmission to vectors is limited by the population density of vectors when dealing with woodrats, but by that of hosts when dealing with raccoons and opossums, while the predation of hosts on vectors which drives oral transmission to hosts is limited by the population density of hosts. Confidence in these conclusions is limited by a severe paucity of data underlying associated parameter estimates, but the approaches developed here can also be applied to the study of other vector-borne infections

    Substrate-Mediated Oxygen Activation by Homoprotocatechuate 2,3-Dioxygenase: Intermediates Formed by a Tyrosine 257 Variant

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    Homoprotocatechuate (HPCA; 3,4-dihydroxyphenylacetate or 4-carboxymethyl catechol) and O(2) bind in adjacent ligand sites of the active site Fe(II) of Homoprotocatechuate 2,3-Dioxygenase (FeHPCD). We have proposed that electron transfer from the chelated aromatic substrate through the Fe(II) to O(2) gives both substrates radical character. This would promote reaction between the substrates to form an alkylperoxo intermediate as the first step in aromatic ring cleavage. Several active site amino acids are thought to promote these reactions through acid/base chemistry, hydrogen bonding, and electrostatic interactions. Here the role of Tyr257 is explored by using the Tyr257Phe (Y257F) variant, which decreases k(cat) by about 75%. The crystal structure of the FeHPCD-HPCA complex has shown that Tyr257 hydrogen bonds to the deprotonated C2-hydroxyl of HPCA. Stopped-flow studies show that at least two reaction intermediates, termed [Formula: see text] and [Formula: see text] , accumulate during the Y257F-HPCA + O(2) reaction prior to formation of the ring-cleaved product. [Formula: see text] is colorless and is formed as O(2) binds reversibly to the HPCA-enzyme complex. [Formula: see text] forms spontaneously from [Formula: see text] and displays a chromophore at 425 nm (ε(425) = 10,500 M-1 cm(−1)). Mössbauer spectra of the intermediates trapped by rapid freeze quench show that both intermediates contain Fe(II). The lack of a chromophore characteristic of a quinone or semiquinone form of HPCA, the presence of Fe(II), and the low O(2) affinity suggests that [Formula: see text] is an HPCA-Fe(II)-O(2) complex with little electron delocalization onto the O(2). In contrast, the intense spectrum of [Formula: see text] suggests the intermediate is most likely an HPCA quinone-Fe(II)-(hydro)peroxo species. Steady-state and transient kinetic analyses show that steps of the catalytic cycle are slowed by as much as 100-fold by the mutation. These effects can be rationalized by a failure of Y257F to facilitate the observed distortion of the bound HPCA that is proposed to promote transfer of one electron to O(2)