45 research outputs found

    The effects of compression on single and multiphase flow in a model polymer electrolyte membrane fuel cell gas diffusion layer

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    A two-dimensional study of an idealised fibrous medium representing the gas diffusion layer of a PEMFC is conducted using computational fluid dynamics. Beginning with an isotropic case the medium is compressed uni-directionally to observe the effects on single and multiphase flow. Relations between the compression ratio and the permeability of the medium are deduced and key parameters dictating the changes in flow are elucidated. The main conclusions are that whilst compression reduces the absolute permeability of an isotropic medium, the creation of anisotropic geometry results in preferential liquid water pathways. The most important parameter for capillary flow, in uniformly hydrophobic media, is the minimum fibre spacing normal to the flow path. The effect is less pronounced with decreasing contact angle and non-existent for neutrally wettable media

    C-3 branched δ-3,5-cis- and trans-THF sugar amino acids: synthesis of the first generation of branched homooligomers.

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    This article describes the efficient synthesis of the first generation of branched sugar amino acid (SAA) oligomers in solution phase via two main routes: by the use of a standard coupling reagent and via the use of active ester intermediates. Benzyl-protected dimeric carbopeptoid and methyl-protected dimeric and tetrameric, hexameric and octameric carbopeptoids were obtained from a branched δ-3,5-trans-tetrahydrofuran (THF) SAA and methyl-protected dimeric and tetrameric carbopeptoids were synthesised from a branched δ-3,5-cis-THF SAA. These systems are of interest because of their potential to display foldameric properties reminiscent of those observed in α-peptides and proteins. Amongst their many uses, foldamers provide simpler models in the study of the factors which induce the folding and unfolding of proteins and, ultimately, potential insights into their functioning

    Carbon-branched delta-tetrahydrofuran sugar amino acids (SAAs) as dipeptide isostere scaffolds

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    The synthesis of the first branched sugar amino acid (SAA) scaffolds [methyl (3R,4R,5R)-5-azidomethyl-3,4-dihydroxy-tetrahydrofuran-3-carboxylate and methyl (3R,4R,5S)-5-azidomethyl-3,4-dihydroxy-tetrahydrofuran-3-carboxylate] by an efficient intramolecular displacement of a highly hindered neopentyl triflate allows access to enantiopure THF derivatives which have carbon substituents. © 2008 Elsevier Ltd. All rights reserved

    Secondary structure in oligomers of carbohydrate amino acids

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    Short oligomeric chains of tetrahydrofuran amino acids exhibit a novel repeating β-turn type secondary structure in solution stabilised by hydrogen bonds and provide clear evidence that carbopeptoids will allow control of conformation in peptidomimetics

    Isopropyl 6-amino-2,5-anhydro-6-N-(2,5anhydro-6-azido-3,6-dideoxy-L-lyxo-hexonyl)-3,6-dideoxy-L-lyxo-hexonate 2.5-hydrate

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    The title compound, C15H24N4O7·2.5H2O, was crystallized with great difficulty from an aqueous solution after several months at 278 K. The crystal structure contains two independent mol-ecules in the asymmetric unit, together with five mol-ecules of water. The independent mol-ecules, which have a very similar geometry, are related by a non-crystallographic pseudo-twofold rotation axis approximately perpendicular to the bc plane. Some intra-molecular hydrogen bonds are present in both of the independent mol-ecules. Moreover, the water mol-ecules play a key role in the formation of a hydrogen-bond network. © International Union of Crystallography 2007
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