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The Advanced Topographic Laser Altimetry System (ATLAS) is the sole instrument on the Ice, Cloud, and land Elevation Satellite 2 (ICESat-2). Without some method of reducing the transmitted data, the volume of ATLAS telemetry would far exceed the normal X-band downlink capability or require many more ground station contacts. The ATLAS Onboard Flight Science Receiver Algorithms (hereinafter Receiver Algorithms or Algorithms) control the amount of science data that is telemetered from the instrument, limiting the data volume by distinguishing surface echoes from background noise, and allowing the instrument to telemeter data from only a small vertical region about the signal. This is accomplished through the transfer of the spacecraft's location and attitude to the instrument every second, use of an onboard Digital Elevation Model, implementation of signal processing techniques, and use of onboard relief and surface type reference maps. Extensive ground testing verified the performance of the Algorithms. On-orbit analysis shows that the Algorithms are working as expected from the ground testing; they are performing well and meeting the mission requirements.
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Recent progress in the domain of time and frequency (T/F) standards requires important improvements of existing time distribution links. Among these, the accuracy of time transfer is actually an important part of the concerns in order to establish and maintain time & space references from ground and/or space facilities. Several time transfers by laser link projects have been carried out over the past 10 years with numerous scientific and metrological objectives. Satellite Laser ranging (SLR) has proven to be a fundamental tool, offering a straightforward, conceptually simple, highly accurate and unambiguous observable. Depending on the mission, LR is used to transmit time over two-way or one-way distances from 500 to several millions of km. The following missions and their objectives employed this technique: European Laser Timing (ELT) at 450 km, Time Transfer by Laser Link (T2L2) at 1,336 km, Laser Time Transfer (LTT) at 36,000 km, Lunar Reconnaissance Orbiter (LRO) at 350,000 km, and MErcury Surface, Space ENvironment, GEochemistry, and Ranging (MESSENGER) at tens of million km. This article describes the synergy between SLR and T/F technologies developed on the ground and in space and as well as the state of the art of their exploitation. The performance and sources of limitation of such space missions are analyzed. It shows that current and future challenges lie in the improvement of the time accuracy and stability of the time for ground geodetic observatories. The role of the next generation of SLR systems is emphasized both in space and at ground level, from the point of view of GGOS and valuable exploitation of the synergy between time synchronization, ranging and data transfer.
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NASA maintains and operates a global network of Very Long Baseline Interferometry (VLBI), Satellite Laser Ranging (SLR), and Global Navigation Satellite System (GNSS) ground stations as part of the NASA Space Geodesy Program. The NASA Space Geodesy Network (NSGN) provides the geodetic products that support Earth observations and the related science requirements as outlined by the US National Research Council (NRC 2010, 2018). The Global Geodetic Observing System (GGOS) and the NRC have set an ambitious goal of improving the Terrestrial Reference Frame (TRF) to have an accuracy of 1 millimeter and stability of 0.1 millimeters per year, an order of magnitude beyond current capabilities. NASA and its partners within GGOS are addressing this challenge by planning and implementing modern geodetic stations co-located at existing and new sites around the world. In 2013, NASA demonstrated the performance of its next-generation systems at the prototype next-generation core site at NASA's Goddard Geophysical and Astronomical Observatory in Greenbelt, Maryland. Implementation of a new broadband VLBI station in Hawaii was completed in 2016. NASA is currently implementing new VLBI and SLR stations in Texas and is planning the replacement of its other aging domestic and international legacy stations. In this article, we describe critical gaps in the current global network and discuss how the new NSGN will expand the global geodetic coverage and ultimately improve the geodetic products. We also describe the characteristics of a modern NSGN site and the capabilities of the next-generation NASA SLR and VLBI systems. Finally, we outline the plans for efficiently operating the NSGN by centralizing and automating the operations of the new geodetic stations.
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The Lunar Orbiter Laser Altimeter (LOLA) aboard the Lunar Reconnaissance Orbiter (LRO) has collected nearly seven billion measurements of surface height on the Moon with an absolute accuracy of â¼1 m and a precision of â¼10 cm. Converting time-of-flight laser altimeter measurements to topographic elevations requires accurate knowledge of the laser pointing with respect to the spacecraft body-fixed coordinate system. To that end, we have utilized altimetric crossovers from LOLA, as well as bidirectional observations of the LOLA laser and receiver boresight via an Earth-based laser tracking ground station. Based on a sample of â¼780,000 globally distributed crossovers from the circular-orbit phase of LRO's mission (â¼27 months), we derive corrections to the LOLA laser boresight. These corrections improve the cross-track and along-track agreement of the crossovers by 24% and 33%, respectively, yielding RMS residuals of â¼10 m. Since early in the LRO mission, the bidirectional laser tracking experiments have confirmed a pointing anomaly when the LOLA instrument is facing toward deep space or the night side of the Moon and have allowed the reconstruction of the laser far-field pattern and receiver telescope pointing. By conducting such experiments shortly after launch and nearly eight years later, we have directly measured changes in the laser characteristics and obtained critical data to understand the laser behavior and refine the instrument pointing model. The methods and results presented here are also relevant to the design, fabrication, and operation of future planetary laser altimeters and their long-term behavior in the space environment.
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For over 40 years, NASA's global network of satellite laser ranging (SLR) stations has provided a significant percentage of the global orbital data used to define the International Terrestrial Reference Frame (ITRF). The current NASA legacy network is reaching its end-of-life and a new generation of systems must be ready to take its place. Scientific demands of sub-millimeter precision ranging and the ever-increasing number of tracking targets give aggressive performance requirements to this new generation of systems. Using lessons learned from the legacy systems and the successful development of a prototype station, a new network of SLR stations, called the Space Geodesy Satellite Laser Ranging (SGSLR) systems, is being developed. These will be the state-of-the-art SLR component of NASA's Space Geodesy Project (SGP). Each of SGSLR's nine subsystems has been designed to produce a robust, kilohertz laser ranging system with 24/7 operational capability and with minimal human intervention. SGSLR's data must support the aggressive goals of the Global Geodetic Observing System (GGOS), which are 1 millimeter (mm) position accuracy and 0.1 mm per year stability of the ITRF. This paper will describe the major requirements and accompanying design of the new SGSLR systems, how the systems will be tested, and the expected system performance.
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A general method to separate the major proteins of rat central and peripheral nervous system myelin has been developed. The key step is the initial quantitative removal of the lipids under conditions where the proteins retain their solubility in HPLC solvents. Lipids are removed by a combination of solvent extraction and column chromatography on Sephadex LH-60 in 2-chloroethanol:10 mM HCl (9:1). Proteins are then separated by reversed-phase (RP) HPLC. Samples are applied to a wide pore reversed-phase C-3 column and eluted with a linear gradient of 10-70% 1-propanol in 0.1% trifluoroacetic acid (0-100% B) over a 60-min period. Myelin basic proteins elute between 25 and 30% B, Wolfgram and other high molecular weight proteins at 35-50% B, proteolipid protein at 65-80% B, and P0 glycoprotein at 55-65% B. This elution pattern is consistent with the known relative hydrophobicity of these proteins. Protein recovery for the entire procedure is greater than 74%. Proteolipid and P0 proteins isolated by HPLC contain 2.3 and 1.1 mol of covalently bound fatty acids, respectively. This fatty acid composition is similar to that previously reported using different isolation procedures. The analysis of central and peripheral nervous system myelin proteins by RP-HPLC permits the isolation of purified proteins for structural and metabolic experiments.
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Proteínas da Mielina/isolamento & purificação , Animais , Química Encefálica , Fenômenos Químicos , Química , Cromatografia Gasosa , Cromatografia em Gel , Cromatografia Líquida de Alta Pressão/métodos , Eletroforese em Gel de Poliacrilamida , Ácidos Graxos/análise , Immunoblotting , Nervos Periféricos/análise , RatosRESUMO
Rat brain myelin proteolipid protein (PLP) is known to contain long chain, covalently bound fatty acids. In the course of characterizing the mechanism of acylation, we found that the isolated PLP, in the absence of any membrane fraction, was esterified after incubation with [3H]palmitoyl coenzyme A (CoA). This observation demonstrated that the protein acts as both an acylating enzyme and an acceptor. Thus, acylation occurs by an autocatalytic process. The possibility of a separate acyltransferase that copurifies with PLP was essentially excluded by adding brain subcellular fractions to the reaction mixtures and by changing the isolation procedure. After deacylation, the protein was acylated at a 4-fold greater rate, suggesting that the original sites were reacylated. The palmitoyl-CoA concentration followed Michaelis kinetics, confirming that spontaneous acylation was not occurring. Pulse-chase experiments indicated that the reaction entails net addition of acyl groups. Although fatty acids are bound via an O-ester linkage, free SH groups are required in the reaction. Denaturation of the protein by sodium dodecyl sulfate or heat inhibits the reaction, whereas cerulenin has little or no effect. PO, the major protein in peripheral nerve myelin, is also an acylated protein, but it was not labeled upon incubation of either peripheral myelin or the isolated protein with [3H]palmitoyl-CoA, demonstrating that it is acylated by a different route. Several synthetic peptides derived from PLP sequences with sites known to be acylated in vivo as well as a series of deacylated PLP tryptic peptides were not labeled, indicating that integrity of the protein is required for acylation. Limited proteolysis and peptide mapping showed that the same sites are acylated in vitro or in vivo, suggesting that the autocatalytic acylation reaction is physiological.
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Acil Coenzima A/metabolismo , Encéfalo/metabolismo , Proteínas da Mielina/metabolismo , Palmitoil Coenzima A/metabolismo , Acilação , Animais , Ditiotreitol/farmacologia , Feminino , Cinética , Masculino , Proteínas da Mielina/isolamento & purificação , Proteína Proteolipídica de Mielina , Mapeamento de Peptídeos , Ratos , Frações Subcelulares/metabolismo , Reagentes de Sulfidrila/farmacologia , TripsinaRESUMO
Fatty acyltransferase activity that catalyzes the transfer of palmitic acid from palmitoyl-CoA to the endogenous myelin proteolipid protein has been demonstrated in isolated rat brain myelin. Optimum enzyme activity for the acylation of proteolipid protein was obtained in 0.1% Triton X-100, 2 mM MgCl2, and 1 mM dithiothreitol at a pH of 7.5 and at 37 degrees C. Other detergents had little or no effect on the reaction whereas acylation was completely abolished by sodium dodecyl sulphate (0.1%). Pulse-chase experiments indicated that the reaction involves the net addition of fatty acid to the protein and not a rapid fatty acid exchange. The rate of acylation was linear up to 30 min, indicating that the concentration of endogenous protein acceptor was constant. Under these conditions and at short time periods, the enzyme activity versus acyl-CoA concentration showed a hyperbolic curve. The apparent Km and Vmax for palmitoyl-CoA was 41 microM and 115 pmol/mg protein/min. Similar values were obtained for stearoyl and oleoyl-CoA, whereas myristoyl-CoA showed a lower specificity for the enzyme. The acyl-CoA specificity was also studied in competition experiments using several saturated and unsaturated fatty acid-CoAs. The product of the reaction was identified as myelin proteolipid protein and the fatty acid was shown to be attached to the protein via an ester linkage. Limited proteolysis and peptide mapping showed that the same sites on the proteolipid protein were acylated when the reaction was carried out in isolated myelin preparations or in brain tissue slices, suggesting physiological importance for the in vitro acylation of endogenous myelin proteolipid protein.
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Acil Coenzima A/metabolismo , Proteínas da Mielina/metabolismo , Proteolipídeos/metabolismo , Acilação , Animais , Quimotripsina/metabolismo , Detergentes/farmacologia , Eletroforese em Gel de Poliacrilamida , Ácidos Graxos Dessaturases/metabolismo , Feminino , Concentração de Íons de Hidrogênio , Cinética , Masculino , Palmitoil Coenzima A/metabolismo , Ratos , Temperatura , Tripsina/metabolismoRESUMO
The timing and correlation properties of pulsed laser backscatter from the ocean surface have been measured with a two-color short-pulse laser altimeter. The Nd: YAG laser transmitted 70-and 35-ps wide pulses simultaneously at 532 and 355 nm at nadir, and the time-resolved returns were recorded by a receiver with 800-ps response time. The time-resolved backscatter measured at both 330- and 1291-m altitudes showed little pulse broadening due to the submeter laser spot size. The differential delay of the 355- and 532-nm backscattered waveforms were measured with a rms error of ~75 ps. The change in aircraft altitudes also permitted the change in atmospheric pressure to be estimated by using the two-color technique.
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The acylation of rat brain proteolipid protein (PLP) with tritiated palmitic, oleic, and myristic acids was studied in vivo and in vitro and compared with the acylation of lipids. Twenty-four hours after intracranial injection of [3H]myristic acid, only 16% of the PLP-bound label appeared as myristic acid, with 66% as palmitic, 9% as stearic, and 6% as oleic acid, whereas greater than 63% of the label in total or myelin phospholipid was in the form of myristic acid. In contrast, after labelling with [3H]palmitic or oleic acids, 75% and 86%, respectively, of the radioactivity in PLP remained in the original form. When brain tissue slices were incubated for short periods of time, the incorporation of palmitic and oleic acids into PLP exceeded that of myristic acid by a factor of 8. In both systems and with all precursors studied, the label associated with PLP was shown to be in ester linkage. The results suggest a preferential acylation of PLP with palmitic and oleic acids as compared with myristic acid. This is consistent with the fatty acid composition of the isolated PLP.