A Combustion Research Facility for Testing Advanced Materials for Space Applications

The test facility presented herein uses a groundbased rocket combustor to test the durability of new ceramic composite and metallic materials in a rocket engine thermal environment. A gaseous H2/02 rocket combustor (essentially a ground-based rocket engine) is used to generate a high temperature/high heat flux environment to which advanced ceramic and/or metallic materials are exposed. These materials can either be an integral part of the combustor (nozzle, thrust chamber etc) or can be mounted downstream of the combustor in the combustor exhaust plume. The test materials can be uncooled, water cooled or cooled with gaseous hydrogen

NASA Innovative Advanced Concepts (NIAC) Phase 1 Final Report: Venus Landsailer Zephyr

Imagine sailing across the hot plains of Venus! A design for a craft to do just this was completed by the COncurrent Multidisciplinary Preliminary Assessment of Space Systems (COMPASS) Team for the NASA Innovative Advanced Concepts (NIAC) project. The robotic craft could explore over 30 km of surface of Venus, driven by the power of the wind

A Cubesat Asteroid Mission: Propulsion Trade-offs

A conceptual design was performed for a 6-U cubesat for a technology demonstration to be launched on the NASA Space Launch System (SLS) test launch EM-1, to be launched into a free-return translunar trajectory. The mission purpose was to demonstrate use of electric propulsion systems on a small satellite platform. The candidate objective chosen was a mission to visit a Near-Earth asteroid. Both asteroid fly-by and asteroid rendezvous missions were analyzed. Propulsion systems analyzed included cold-gas thruster systems, Hall and ion thrusters, incorporating either Xenon or Iodine propellant, and an electrospray thruster. The mission takes advantage of the ability of the SLS launch to place it into an initial trajectory of C3=0

Key features determining the specificity of aspartic proteinase inhibition by the helix-forming IA3 polypeptide

The 68-residue IA3 polypeptide from Saccharomyces cerevisiae is essentially unstructured. It inhibits its target aspartic proteinase through an unprecedented mechanism whereby residues 2–32 of the polypeptide adopt an amphipathic -helical conformation upon contact with the active site of the enzyme. This potent inhibitor (Ki < 0.1 nM) appears to be specific for a single target proteinase, saccharopepsin. Mutagenesis of IA3 from S. cerevisiae and its ortholog from Saccharomyces castellii was coupled with quantitation of the interaction for each mutant polypeptide with saccharopepsin and closely related aspartic proteinases from Pichia pastoris and Aspergillus fumigatus. This identified the charged K18/D22 residues on the otherwise hydrophobic face of the amphipathic helix as key selectivity-determining residues within the inhibitor and implicated certain residues within saccharopepsin as being potentially crucial. Mutation of these amino acids established Ala-213 as the dominant specificity-governing feature in the proteinase. The side chain of Ala-213 in conjunction with valine 26 of the inhibitor marshals Tyr-189 of the enzyme precisely into a position in which its side-chain hydroxyl is interconnected via a series of water-mediated contacts to the key K18/D22 residues of the inhibitor. This extensive hydrogen bond network also connects K18/D22 directly to the catalytic Asp-32 and Tyr-75 residues of the enzyme, thus deadlocking the inhibitor in position. In most other aspartic proteinases, the amino acid at position 213 is a larger hydrophobic residue that prohibits this precise juxtaposition of residues and eliminates these enzymes as targets of IA3. The exquisite specificity exhibited by this inhibitor in its interaction with its cognate folding partner proteinase can thus be readily explained