5 research outputs found

    Orbital Debris Assesment Tesing in the AEDC Range G

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    The space environment presents many hazards for satellites and spacecraft. One of the major hazards is hypervelocity impacts from uncontrolled man-made space debris. Arnold Engineering Development Complex (AEDC), The National Aeronautics and Space Administration (NASA), The United States Air Force Space and Missile Systems Center (SMC), the University of Florida, and The Aerospace Corporation configured a large ballistic range to perform a series of hypervelocity destructive impact tests in order to better understand the effects of space collisions. The test utilized AEDC's Range G light gas launcher, which is capable of firing projectiles up to 7 km/s. A non-functional full-scale representation of a modern satellite called the DebriSat was destroyed in the enclosed range enviroment. Several modifications to the range facility were made to ensure quality data was obtained from the impact events. The facility modifcations were intended to provide a high impact energy to target mass ratio (>200 J/g), a non-damaging method of debris collection, and an instrumentation suite capable of providing information on the physics of the entire imapct event

    Whitefield News

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    File includes: January 2017 Volume 4, Issue 7 February 2017 Volume 4, Issue 8 March 2017 Volume 4, Issue 9 April 2017 Volume 4, Issue 10 May 2017 Volume 4, Issue 11 June 2017 Volume 4, Issue 12 July 2017 Volume 5, Issue 1 August 2017 Volume 5, Issue 2 September 2017 Volume 5, Issue 3 October 2017 Volume 5, Issue 4 November 2017 Volume 5, Issue 5 December 2017 Volume 5, Issue

    Physical and Functional Interactions between the Herpes Simplex Virus UL15 and UL28 DNA Cleavage and Packaging Proteins

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    Herpes simplex virus (HSV) DNA is cleaved from concatemers and packaged into capsids in infected cell nuclei. This process requires seven viral proteins, including UL15 and UL28. UL15 expressed alone displays a nuclear localization, while UL28 remains cytoplasmic. Coexpression with UL15 enables UL28 to enter nuclei, suggesting an interaction between the two proteins. Additionally, UL28 copurified with UL15 from HSV-infected cells after ion-exchange and DNA affinity chromatography, and the complex sedimented as a 1:1 heterodimer upon sucrose gradient centrifugation. These findings are evidence of a physical interaction of UL15 and UL28 and a functional role for UL15 in directing UL28 to the nucleus
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