1,699 research outputs found

    Low-altitude measurements of 2ā€“6 MeV electron trapping lifetimes at 1.5 ā‰¤ L ā‰¤ 2.5

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    During the Halloween Storm period (Octoberā€“November 2003), a new Van Allen belt electron population was powerfully accelerated. The inner belt of electrons formed in this process decayed over a period of days to years. We have examined quantitatively the decay rates for electrons seen in the region of 1.5 ā‰¤ L ā‰¤ 2.5 using SAMPEX satellite observations. At L = 1.5 the e-folding lifetime for 2ā€“6 MeV electrons was Ļ„ āˆ¼ 180 days. On the other hand, for the half-dozen distinct acceleration (or enhancement) events seen during late-2003 through 2005 at L āˆ¼ 2.0, the lifetimes ranged from Ļ„ āˆ¼ 8 days to Ļ„ āˆ¼ 35 days. We compare these loss rates to those expected from prior studies. We find that lifetimes at L = 2.0 are much shorter than the average 100ā€“200 days that present theoretical estimates would suggest for the overall L = 2 electron population. Additional wave-particle interaction aspects must be included in theoretical treatments and we describe such possibilities here

    Mutations in the Arabidopsis Peroxisomal ABC Transporter COMATOSE Allow Differentiation between Multiple Functions In Planta: Insights from an Allelic Series

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    COMATOSE (CTS), the Arabidopsis homologue of human Adrenoleukodystrophy protein (ALDP), is required for import of substrates for peroxisomal Ī²-oxidation. A new allelic series and a homology model based on the bacterial ABC transporter, Sav1866, provide novel insights into structure-function relations of ABC subfamily D proteins. In contrast to ALDP, where the majority of mutations result in protein absence from the peroxisomal membrane, all CTS mutants produced stable protein. Mutation of conserved residues in the Walker A and B motifs in CTS nucleotide-binding domain (NBD) 1 resulted in a null phenotype but had little effect in NBD2, indicating that the NBDs are functionally distinct in vivo. Two alleles containing mutations in NBD1 outside the Walker motifs (E617K and C631Y) exhibited resistance to auxin precursors 2,4-dichlorophenoxybutyric acid (2,4-DB) and indole butyric acid (IBA) but were wild type in all other tests. The homology model predicted that the transmission interfaces are domain-swapped in CTS, and the differential effects of mutations in the conserved "EAA motif" of coupling helix 2 supported this prediction, consistent with distinct roles for each NBD. Our findings demonstrate that CTS functions can be separated by mutagenesis and the structural model provides a framework for interpretation of phenotypic data
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