A magnetic shield/dual purpose mission

The objective of this work is to design, build, and fly a dual-purpose payload whose function is to produce a large volume, low intensity magnetic field and to test the concept of using such a magnetic field to protect manned spacecraft against particle radiation. An additional mission objective is to study the effect of this moving field on upper atmosphere plasmas. Both mission objectives appear to be capable of being tested using the same superconducting coil. The potential benefits of this magnetic shield concept apply directly to both earth-orbital and interplanetary missions. This payload would be a first step in assessing the true potential of large volume magnetic fields in the U.S. space program. Either converted launch systems or piggyback payload opportunities may be appropriate for this mission. The use of superconducting coils for magnetic shielding against solar flare radiation during manned interplanetary missions has long been contemplated and was considered in detail in the years preceding the Apollo mission. With the advent of new superconductors, it has now become realistic to reconsider this concept for a Mars mission. Even in near-earth orbits, large volume magnetic fields produced using conventional metallic superconductors allow novel plasma physics experiments to be contemplated. Both deployed field-coil and non-deployed field-coil shielding arrangements have been investigated, with the latter being most suitable for an initial test payload in a polar orbit

Development of NEXRAD Wind Retrievals as Input to Atmospheric Dispersion Models

The objective of this study is to determine the feasibility that routinely collected data from the Doppler radars can appropriately be used in Atmospheric Dispersion Models (ADMs) for emergency response. We have evaluated the computational efficiency and accuracy of two variational mathematical techniques that derive the u- and v-components of the wind from radial velocities obtained from Doppler radars. A review of the scientific literature indicated that the techniques employ significantly different approaches in applying the variational techniques: 2-D Variational (2DVar), developed by NOAA¹s (National Oceanic and Atmospheric Administration's) National Severe Storms Laboratory (NSSL) and Variational Doppler Radar Analysis System (VDRAS), developed by the National Center for Atmospheric Research (NCAR). We designed a series of numerical experiments in which both models employed the same horizontal domain and resolution encompassing Oklahoma City for a two-week period during the summer of 2003 so that the computed wind retrievals could be fairly compared. Both models ran faster than real-time on a typical single dual-processor computer, indicating that they could be used to generate wind retrievals in near real-time. 2DVar executed ~2.5 times faster than VDRAS because of its simpler approach

Analysis of jak2 catalytic function by peptide microarrays: The role of the JH2 domain and V617F mutation

Janus kinase 2 (JAK2) initiates signaling from several cytokine receptors and is required for biological responses such as erythropoiesis. JAK2 activity is controlled by regulatory proteins such as Suppressor of Cytokine Signaling (SOCS) proteins and protein tyrosine phosphatases. JAK2 activity is also intrinsically controlled by regulatory domains, where the pseudokinase (JAK homology 2, JH2) domain has been shown to play an essential role. The physiological role of the JH2 domain in the regulation of JAK2 activity was highlighted by the discovery of the acquired missense point mutation V617F in myeloproliferative neoplasms (MPN). Hence, determining the precise role of this domain is critical for understanding disease pathogenesis and design of new treatment modalities. Here, we have evaluated the effect of inter-domain interactions in kinase activity and substrate specificity. By using for the first time purified recombinant JAK2 proteins and a novel peptide micro-array platform, we have determined initial phosphorylation rates and peptide substrate preference for the recombinant kinase domain (JH1) of JAK2, and two constructs comprising both the kinase and pseudokinase domains (JH1-JH2) of JAK2. The data demonstrate that (i) JH2 drastically decreases the activity of the JAK2 JH1 domain, (ii) JH2 increased the Kmfor ATP (iii) JH2 modulates the peptide preference of JAK2 (iv) the V617F mutation partially releases this inhibitory mechanism but does not significantly affect substrate preference or Kmfor ATP. These results provide the biochemical basis for understanding the interaction between the kinase and the pseudokinase domain of JAK2 and identify a novel regulatory role for the JAK2 pseudokinase domain. Additionally, this method can be used to identify new regulatory mechanisms for protein kinases that provide a better platform for designing specific strategies for therapeutic approaches

Finishing the euchromatic sequence of the human genome

The sequence of the human genome encodes the genetic instructions for human physiology, as well as rich information about human evolution. In 2001, the International Human Genome Sequencing Consortium reported a draft sequence of the euchromatic portion of the human genome. Since then, the international collaboration has worked to convert this draft into a genome sequence with high accuracy and nearly complete coverage. Here, we report the result of this finishing process. The current genome sequence (Build 35) contains 2.85 billion nucleotides interrupted by only 341 gaps. It covers ∼99% of the euchromatic genome and is accurate to an error rate of ∼1 event per 100,000 bases. Many of the remaining euchromatic gaps are associated with segmental duplications and will require focused work with new methods. The near-complete sequence, the first for a vertebrate, greatly improves the precision of biological analyses of the human genome including studies of gene number, birth and death. Notably, the human enome seems to encode only 20,000-25,000 protein-coding genes. The genome sequence reported here should serve as a firm foundation for biomedical research in the decades ahead