The Modeling of Roughness Effect on the Performance of a Controlled Diffusion Airfoil

peer reviewedThe manufacturing and operational roughness of aerodynamic profiles impacts both the laminar and the turbulent boundary layers state, directly affecting the aerodynamic and thermal performance of typical turbomachinery components. By better understanding the underlying physical mechanisms, the present work aims at building a more refined and comprehensive model to take the effects of surface finish into account. The model is implemented into the MIT Multiple Blade Interacting Streamtube Euler Solver (MISES) and is validated against experimental results for different roughness levels, Reynolds number, and Mach number regimes. In the proposed model, the roughness effects on the turbulent boundary layer (BL) state are included through the modification of the turbulent skin friction law, while the roughness level is implemented through a new definition of ks that accounts for the influence of the roughness skewness. Particular emphasis is placed on the modeling of the transitionally rough regime. Finally, roughness effects on transition are modeled by implementing the Mayle rough-induced onset transition criterion. Results are validated in terms of the total pressure loss coefficient and the outlet flow angle, leading to a marked improvement in terms of agreement with the experimental data

Molecular evolution of the CYTH superfamily of proteins

Molecular evolution of the CYTH superfamily of proteins L. Bettendorff, D. Delvaux, G. Kohn, P. Wins, B. Lakaye GIGA-Neurosciences, University of Liège, Belgium The CYTH superfamily of proteins was named after the two founding members, the CYaB adenylyl cyclase from Aeromonas hydrophila and the human 25-kDa THiamine triphosphatase (ThTPase). Members of this superfamily of proteins exist in all organisms including bacteria, archaea, plants and animals (except in birds) and can be traced back to the Last Universal Common Ancestor. They are characterized by a consensus sequence including several charged residues involved in divalent cation and triphosphate binding. Indeed, all members of the CYTH family that are characterized act on triphosphate derivatives and require at least one divalent cation for catalysis. The Nitrosomonas europaea (1) and E.coli CYTH proteins are specific inorganic triphosphatases. We propose that inorganic triphosphate (PPPi), the most simple triphosphate compound that can be imagined, is the primitive substrate of CYTH proteins. Other enzyme activities such as adenylate cyclase (in A. hydrophila), mRNA triphosphatase (in fungi and protozoans) and ThTPase (in metazoans) activities are secondary acquisitions. We show that ThTPase activity is not limited to mammals, but Sea anemone and Zebrafish CYTH proteins are already specific ThTPases and the acquisition of this enzyme activity is linked to the presence of a Trp (W53 in mammalian ThTPases) residue involved in the binding of the thiazole heterocycle of the thiamine molecule. The importance of W53 for the specificity of mammalian ThTPases is confirmed by site-directed mutagenesis. Furthermore, we propose a conserved catalytic mechanism between inorganic triphosphatases and ThTPases, based on a catalytic dyad comprising a Lys and a Tyr residue, explaining the alkaline pH optimum of CYTH proteins. (1) Delvaux et al. J. Biol. Chem 286 (2011) 34023-3

Structural Determinants of Specificity and Catalytic Mechanism in mammalian 25-kDa Thiamine Triphosphatase

Background: Thiamine triphosphate (ThTP) is present in most organisms and might be involved in intracellular signaling. In mammalian cells, the cytosolic ThTP level is controlled by a specific thiamine triphosphatase (ThTPase), belonging to the CYTH superfamily of proteins. CYTH proteins are present in all superkingdoms of life and act on various triphosphorylated substrates. Methods: Using crystallography, mass spectrometry and mutational analysis, we identified the key structural determinants of the high specificity and catalytic efficiency of mammalian ThTPase. Results: Triphosphate binding requires three conserved arginines while the catalytic mechanism relies on an unusual lysine-tyrosine dyad. By docking of the ThTP molecule in the active site, we found that Trp-53 should interact with the thiazole part of the substrate molecule, thus playing a key role in substrate recognition and specificity. Sea anemone and zebrafish CYTH proteins, which retain the corresponding Trp residue, are also specific ThTPases. Surprisingly, the whole chromosome region containing the ThTPase gene is lost in birds. Conclusion: The specificity for ThTP is linked to a stacking interaction between the thiazole heterocycle of thiamine and a tryptophan residue. The latter likely plays a key role in the secondary acquisition of ThTPase activity in early metazoan CYTH enzymes, in the lineage leading from cnidarians to mammals. General significance: We show that ThTPase activity is not restricted to mammals as previously thought but is an acquisition of early metazoans. This, and the identification of critically important residues, allows us to draw an evolutionary perspective of the CYTH family of proteins

La sécurité de l'individu numérisé: réflexions prospectives et internationales : actes du colloque du programme de recherche Asphales, ACI-Informatique, Paris, 22 et 23 novembre 2007

Actes interdisciplinaires du colloque terminal du programme ASPHALESNational audienc