3,605 research outputs found

    Assessment team report on flight-critical systems research at NASA Langley Research Center

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    The quality, coverage, and distribution of effort of the flight-critical systems research program at NASA Langley Research Center was assessed. Within the scope of the Assessment Team's review, the research program was found to be very sound. All tasks under the current research program were at least partially addressing the industry needs. General recommendations made were to expand the program resources to provide additional coverage of high priority industry needs, including operations and maintenance, and to focus the program on an actual hardware and software system that is under development

    Current investment practices of New England life insurance companies

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    Thesis (M.B.A.)--Boston Universit

    Low-speed wind-tunnel tests of an advanced eight-bladed propeller

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    As part of a research program on advanced turboprop aircraft aerodynamics, a low-speed wind-tunnel investigation was conducted to document the basic performance and force and moment characteristics of an advanced eight-bladed propeller. The results show that in addition to the normal force and pitching moment produced by the propeller/nacelle combination at angle of attack, a significant side force and yawing moment are also produced. Furthermore, it is shown that for test conditions wherein compressibility effects can be ignored, accurate simulation of propeller performance and flow fields can be achieved by matching the nondimensional power loading of the model propeller to that of the full-scale propeller

    MF890

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    Edward P. Call & James R. Dunham, A guide to successful AI, Kansas State University, September 1992

    Nature’s Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases

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    Iron is an especially important redox-active cofactor in biology because of its ability to mediate reactions with atmospheric O₂. Iron-dependent oxygenases exploit this earth-abundant transition metal for the insertion of oxygen atoms into organic compounds. Throughout the astounding diversity of transformations catalyzed by these enzymes, the protein framework directs reactive intermediates toward the precise formation of products, which, in many cases, necessitates the cleavage of strong C–H bonds. In recent years, members of several iron-dependent oxygenase families have been engineered for new-to-nature transformations that offer advantages over conventional synthetic methods. In this Perspective, we first explore what is known about the reactivity of heme-dependent cytochrome P450 oxygenases and nonheme iron-dependent oxygenases bearing the 2-His-1-carboxylate facial triad by reviewing mechanistic studies with an emphasis on how the protein scaffold maximizes the catalytic potential of the iron-heme and iron cofactors. We then review how these cofactors have been repurposed for abiological transformations by engineering the protein frameworks of these enzymes. Finally, we discuss contemporary challenges associated with engineering these platforms and comment on their roles in biocatalysis moving forward

    Nature’s Machinery, Repurposed: Expanding the Repertoire of Iron-Dependent Oxygenases

    Get PDF
    Iron is an especially important redox-active cofactor in biology because of its ability to mediate reactions with atmospheric O₂. Iron-dependent oxygenases exploit this earth-abundant transition metal for the insertion of oxygen atoms into organic compounds. Throughout the astounding diversity of transformations catalyzed by these enzymes, the protein framework directs reactive intermediates toward the precise formation of products, which, in many cases, necessitates the cleavage of strong C–H bonds. In recent years, members of several iron-dependent oxygenase families have been engineered for new-to-nature transformations that offer advantages over conventional synthetic methods. In this Perspective, we first explore what is known about the reactivity of heme-dependent cytochrome P450 oxygenases and nonheme iron-dependent oxygenases bearing the 2-His-1-carboxylate facial triad by reviewing mechanistic studies with an emphasis on how the protein scaffold maximizes the catalytic potential of the iron-heme and iron cofactors. We then review how these cofactors have been repurposed for abiological transformations by engineering the protein frameworks of these enzymes. Finally, we discuss contemporary challenges associated with engineering these platforms and comment on their roles in biocatalysis moving forward
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