Vertical Distribution of Aersols and Water Vapor Using CRISM Limb Observations

Near-infrared spectra taken in a limb-viewing geometry by the Compact Reconnaissance Imaging Spectrometer for Mars (CRISM) on-board the Mars Reconnaissance Orbiter (MRO) provide a useful tool for probing atmospheric structure. Specifically, the observed radiance as a function of wavelength and height above the limb allows the vertical distribution of both dust and ice aerosols to be retrieved. These data serve as an important supplement to the aerosol profiling provided by the MRO/MCS instrument allowing independent validation and giving additional information on particle physical and scattering properties through multi-wavelength studies. A total of at least ten CRISM limb observations have been taken so far covering a full Martian year. Each set of limb observations nominally contains about four dozen scans across the limb giving pole-to-pole coverage for two orbits at roughly 100 and 290 W longitude over the Tharsis and Syrtis/Hellas regions, respectively. At each longitude, limb scans are spaced roughly 10 degrees apart in latitude, with a vertical spatial resolution on the limb of roughly 800 m. Radiative transfer modeling is used to model the observations. We compute synthetic CRISM limb spectra using a discrete-ordinates radiative transfer code that accounts for multiple scattering from aerosols and accounts for spherical geometry of the limb observations by integrating the source functions along curved paths in that coordinate system. Retrieved are 14-point vertical profiles for dust and water ice aerosols with resolution of 0.4 scale heights between one and six scale heights above the surface. After the aerosol retrieval is completed, the abundances of C02 (or surface pressure) and H20 gas are retrieved by matching the depth of absorption bands at 2000 nm for carbon dioxide and at 2600 run for water vapor. In addition to the column abundance of water vapor, limited information on its vertical structure can also be retrieved depending on the signal available from aerosol scattering

Variational Trajectory Optimization Tool Set: Technical description and user's manual

The algorithms that comprise the Variational Trajectory Optimization Tool Set (VTOTS) package are briefly described. The VTOTS is a software package for solving nonlinear constrained optimal control problems from a wide range of engineering and scientific disciplines. The VTOTS package was specifically designed to minimize the amount of user programming; in fact, for problems that may be expressed in terms of analytical functions, the user needs only to define the problem in terms of symbolic variables. This version of the VTOTS does not support tabular data; thus, problems must be expressed in terms of analytical functions. The VTOTS package consists of two methods for solving nonlinear optimal control problems: a time-domain finite-element algorithm and a multiple shooting algorithm. These two algorithms, under the VTOTS package, may be run independently or jointly. The finite-element algorithm generates approximate solutions, whereas the shooting algorithm provides a more accurate solution to the optimization problem. A user's manual, some examples with results, and a brief description of the individual subroutines are included

Chicora research contribution 264

This survey was done to assess the archaeological significance of the site

CRISM Observations of Water Vapor and Carbon Monoxide

Near-infrared spectra returned by the Compact Reconnaissance Imaging Spectrometer for Mars (CRISM, [1]) on-board the Mars Reconnaissance Orbiter (MRO) contain the clear spectral signature of several atmospheric gases including carbon dioxide (CO2), water vapor (H2O), and carbon monoxide (CO). Here we describe the seasonal and spatial mapping of water vapor and carbon dioxide for one full Martian year using CRISM spectra

Familial Alzheimer’s disease mutations in amyloid protein precursor alter proteolysis by γ-secretase to increase amyloid β-peptides of ≥45 residues

Production of amyloid β-protein (Aβ) is carried out by the membrane-embedded γ-secretase complex. Mutations in the transmembrane domain of amyloid β-protein precursor (APP) associated with early-onset familial Alzheimer's disease (FAD) can alter the ratio of aggregation-prone 42-residue Aβ (Aβ42) to 40-residue Aβ (Aβ40). However, APP substrate is proteolyzed processively by γ-secretase along two pathways: Aβ49→Aβ46→Aβ43→Aβ40 and Aβ48→Aβ45→Aβ42→Aβ38. Effects of FAD mutations on each proteolytic step are unknown, largely due to difficulties in detecting and quantifying longer Aβ peptides. To address this, we carried out systematic and quantitative analyses of all tri- and tetrapeptide coproducts from proteolysis of wild-type and 14 FAD-mutant APP substrates by purified γ-secretase. These small peptides, including FAD-mutant forms, were detected by tandem mass spectrometry and quantified by establishing concentration curves for each of 32 standards. APP intracellular domain (AICD) coproducts were quantified by immunoblot, and the ratio of AICD products corresponding to Aβ48 and Aβ49 was determined by mass spectrometry. Levels of individual Aβ peptides were determined by subtracting levels of peptide coproducts associated with degradation from those associated with production. This method was validated for Aβ40 and Aβ42 by specific ELISAs and production of equimolar levels of Aβ and AICD. Not all mutant substrates led to increased Aβ42/40. However, all 14 disease-causing mutations led to inefficient processing of longer forms of Aβ ≥ 45 residues. In addition, the effects of certain mutations provided insight into the mechanism of processive proteolysis: intermediate Aβ peptides apparently remain bound for subsequent trimming and are not released and reassociated