Seabasing and joint expeditionary logistics

Student Integrated ProjectIncludes supplementary material. Executive Summary and Presentation.Recent conflicts such as Operation Desert Shield/Storm and Operation Iraqi Freedom highlight the logistics difficulties the United States faces by relying on foreign access and infrastructure and large supply stockpiles ashore to support expeditionary operations. The Navy's transformational vision for the future, Sea Power 21, involves Seabasing as a way to address these difficulties by projecting and sustaining joint forces globally from the sea. This study analyzes logistics flow to, within and from a Sea Base to an objective, and the architectures and systems needed to rapidly deploy and sustain a brigade-size force. Utilizing the Joint Capabilities Integration and Development System (JCIDS), this study incorporates a systems engineering framework to examine current systems, programs of record and proposed systems out to the year 2025. Several capability gaps that hamper a brigade-size force from seizing the initiative anywhere in the world within a 10-day period point to a need for dedicated lift assets, such as high-speed surface ships or lighter-than-air ships, to facilitate the rapid formation of the Sea Base. Additionally, the study identifies the need for large-payload/high-speed or load-once/direct-to- objective connector capabilities to minimize the number of at-sea transfers required to employ such a force from the Sea Base in 10 hrs. With these gaps addressed, the Joint Expeditionary Brigade is supportable from the Sea Base.http://archive.org/details/seabasingndjoint109456918N

Glycerol kinase from Escherichia coli and an Ala65→Thr mutant: the crystal structures reveal conformational changes with implications for allosteric regulation

AbstractBackground: Glycerol kinase (GK) from Escherichia coli is a velocity-modulated (V system) enzyme that has three allosteric effectors with independent mechanisms: fructose-1,6-bisphosphate (FBP); the phosphocarrier protein IIAGlc; and adenosine nucleotides. The enzyme exists in solution as functional dimers that associate reversibly to form tetramers. GK is a member of a superfamily of ATPases that share a common ATPase domain and are thought to undergo a large conformational change as an intrinsic step in their catalytic cycle. Members of this family include actin, hexokinase and the heat shock protein hsc70.Results: We report here the crystal structures of GK and a mutant of GK (Ala65→Thr) in complex with glycerol and ADP. Crystals of both enzymes contain the same 222 symmetric tetramer. The functional dimer is identical to that described previously for the IIAGlc–GK complex structure. The tetramer interface is significantly different, however, with a relative 22.3° rotation and 6.34 å translation of one functional dimer. The overall monomer structure is unchanged except for two regions: the IIAGlc-binding site undergoes a structural rearrangement and residues 230–236 become ordered and bind orthophosphate at the tetramer interface. We also report the structure of a second mutant of GK (IIe474→Asp) in complex with IIAGlc; this complex crystallized isomorphously to the wild type IIAGlc–GK complex. Site-directed mutants of GK with substitutions at the IIAGlc-binding site show significantly altered kinetic and regulatory properties, suggesting that the conformation of the binding site is linked to the regulation of activity.Conclusions: We conclude that the new tetramer structure presented here is an inactive form of the physiologically relevant tetramer. The structure and location of the orthophosphate-binding site is consistent with it being part of the FBP-binding site. Mutational analysis and the structure of the IIAGlc–GK(IIe474→Asp) complex suggest the conformational transition of the IIAGlc-binding site to be an essential aspect of IIAGlc regulation