Heat Capacity Mapping Radiometer (HCMR) data processing algorithm, calibration, and flight performance evaluation

The rationale and procedures used in the radiometric calibration and correction of Heat Capacity Mapping Mission (HCMM) data are presented. Instrument-level testing and calibration of the Heat Capacity Mapping Radiometer (HCMR) were performed by the sensor contractor ITT Aerospace/Optical Division. The principal results are included. From the instrumental characteristics and calibration data obtained during ITT acceptance tests, an algorithm for post-launch processing was developed. Integrated spacecraft-level sensor calibration was performed at Goddard Space Flight Center (GSFC) approximately two months before launch. This calibration provided an opportunity to validate the data calibration algorithm. Instrumental parameters and results of the validation are presented and the performances of the instrument and the data system after launch are examined with respect to the radiometric results. Anomalies and their consequences are discussed. Flight data indicates a loss in sensor sensitivity with time. The loss was shown to be recoverable by an outgassing procedure performed approximately 65 days after the infrared channel was turned on. It is planned to repeat this procedure periodically

Mapping the O-Mannose Glycoproteome in Saccharomyces cerevisiae

O-Mannosylation is a vital protein modification conserved from fungi to humans. Yeast is a perfect model to study this post-translational modification, because in contrast to mammals O-mannosylation is the only type of O-glycosylation. In an essential step toward the full understanding of protein O-mannosylation we mapped the O-mannose glycoproteome in baker's yeast. Taking advantage of an O-glycan elongation deficient yeast strain to simplify sample complexity, we identified over 500 O-glycoproteins from all subcellular compartments for which over 2300 O-mannosylation sites were mapped by electron-transfer dissociation (ETD)-based MS/MS. In this study, we focus on the 293 O-glycoproteins (over 1900 glycosylation sites identified by ETD-MS/MS) that enter the secretory pathway and are targets of ER-localized protein O-mannosyltransferases. We find that O-mannosylation is not only a prominent modification of cell wall and plasma membrane proteins, but also of a large number of proteins from the secretory pathway with crucial functions in protein glycosylation, folding, quality control, and trafficking. The analysis of glycosylation sites revealed that O-mannosylation is favored in unstructured regions and β-strands. Furthermore, O-mannosylation is impeded in the proximity of N-glycosylation sites suggesting the interplay of these types of post-translational modifications. The detailed knowledge of the target proteins and their O-mannosylation sites opens for discovery of new roles of this essential modification in eukaryotes, and for a first glance on the evolution of different types of O-glycosylation from yeast to mammals

Interlaminar Fracture Toughness Evaluation in Glass/Epoxy Composites Using Acoustic Emission and Finite Element Methods

© 2014, ASM International. Delamination is one of the most common modes of failure in laminated composites and it leads to the loss of structural strength and stiffness. In this paper, mode I, mode II, and mixed of these pure modes were investigated using mechanical data, Finite Element Method (FEM) and Acoustic Emission (AE) signals. Experimental data were obtained from insitu monitoring of glass/epoxy laminated composites with different lay-ups when subjected to different modes of failure. The main objective was to investigate the behavior of delamination propagation and to evaluate the critical value of the strain energy which is required for onset of the delamination (GC). For the identification of interlaminar fracture toughness of the specimens, four methods were used: (a) ASTM standard methods, (b) FEM analysis, (c) AE method, and (d) sentry function method which is a function of mechanical and AE behaviors of the specimens. The results showed that the GC values obtained by the sentry function method and FEM analysis were in a close agreement with the results of nonlinearity methods which is recommended in the ASTM standards. It was also found that the specimens under different loading conditions and various lay-up have different GC values. These differences are related to different stress components distribution in the specimens which induce various damage mechanisms. Accordingly, stress components distribution obtained from FEM analyses were in agreement with SEM observations of the damaged surfaces of the specimens

Histoplasma capsulatum Encodes a Dipeptidyl Peptidase Active against the Mammalian Immunoregulatory Peptide, Substance P

The pathogenic fungus Histoplasma capsulatum secretes dipeptidyl peptidase (Dpp) IV enzyme activity and has two putative DPPIV homologs (HcDPPIVA and HcDPPIVB). We previously showed that HcDPPIVB is the gene responsible for the majority of secreted DppIV activity in H. capsulatum culture supernatant, while we could not detect any functional contribution from HcDPPIVA. In order to determine whether HcDPPIVA encodes a functional DppIV enzyme, we expressed HcDPPIVA in Pichia pastoris and purified the recombinant protein. The recombinant enzyme cleaved synthetic DppIV substrates and had similar biochemical properties to other described DppIV enzymes, with temperature and pH optima of 42°C and 8, respectively. Recombinant HcDppIVA cleaved the host immunoregulatory peptide substance P, indicating the enzyme has the potential to affect the immune response during infection. Expression of HcDPPIVA under heterologous regulatory sequences in H. capsulatum resulted in increased secreted DppIV activity, indicating that the encoded protein can be expressed and secreted by its native organism. However, HcDPPIVA was not required for virulence in a murine model of histoplasmosis. This work reports a fungal enzyme that can function to cleave the immunomodulatory host peptide substance P