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Träfflista för sökning "WFRF:(Ferguson T.) srt2:(2000-2004)"

Sökning: WFRF:(Ferguson T.) > (2000-2004)

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  • Allard, F, et al. (författare)
  • Model atmospheres and spectra: The role of dust
  • 2003
  • Ingår i: Proceedings of the International Astronomical Union (Brown Dwarfs). - 0074-1809. - 158381132X ; 211, s. 325-332
  • Konferensbidrag (refereegranskat)abstract
    • Brown dwarf atmospheres form molecules, then high temperature condensates (corundum, titanates, silicates, and iron compounds), and then low temperature condensates (ices) as they cool down over time. These produce large opacities which govern entirely their spectral energy distribution. Just as it is important to know molecular opacities (TiO, H2O, CH4, etc.) with accuracy, it is imperative to understand the interplay of processes (e.g. condensation, sedimentation, coagulation, convection) that determines the radial and size distribution of grains. Limiting case models have shown that young, hot brown (L) dwarfs form dust mostly in equilibrium, while at much cooler stages (late T dwarfs) all high temperature condensates have sedimented out of their photospheres. But this process is gradual and all intermediate classes of brown dwarfs can partly be understood in terms of partial sedimentation of dust. With new models accounting for these processes, we describe the effects they may have upon brown dwarf spectral properties.
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  • van Aalten, DMF, et al. (författare)
  • Binding site differences revealed by crystal structures of Plasmodium falciparum and bovine acyl-CoA binding protein
  • 2001
  • Ingår i: JOURNAL OF MOLECULAR BIOLOGY. - 0022-2836. ; 309:1, s. 181-192
  • Tidskriftsartikel (refereegranskat)abstract
    • Acyl-CoA binding protein (ACBP) maintains a pool of fatty acyl-CoA molecules in the cell and plays a role in fatty acid metabolism. The biochemical properties of Plasmodium falciparum ACBP are described together with the 2.0 A resolution crystal structures of a P. falciparum ACBP-acyl-CoA complex and of bovine ACBP in two crystal forms. Overall, the bovine ACBP crystal structures are similar to the NMR structures published previously; however, the bovine and parasite ACBP structures are less similar. The parasite ACBP is shown to have a different ligand-binding pocket, leading to an acyl-CoA binding specificity different from that of bovine ACBP. Several non-conservative differences in residues that interact with the ligand were identified between the mammalian and parasite ACBPs. These, together with measured binding-specificity differences, suggest that there is a potential for the design of molecules that might selectively block the acyl-CoA binding site.
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