The detector control unit of the fine guidance sensor instrument on-board the ARIEL mission: design status

ARIEL is an ESA mission whose scientific goal is to investigate exoplanetary atmospheres. The payload is composed by two instruments: AIRS (ARIEL IR Spectrometer) and FGS (Fine Guidance System). The FGS detection chain is composed by two HgCdTe detectors and by the cold Front End Electronics (SIDECAR), kept at cryogenic temperatures, interfacing with the F-DCU (FGS Detector Control Unit) boards that we will describe thoroughly in this paper. The F-DCU are situated in the warm side of the payload in a box called FCU (FGS Control Unit) and contribute to the FGS VIS/NIR imaging and NIR spectroscopy. The F-DCU performs several tasks: drives the detectors, processes science data and housekeeping telemetries, manages the commands exchange between the FGS/DPU (Data Processing Unit) and the SIDECARs and provides high quality voltages to the detectors. This paper reports the F-DCU status, describing its architecture, the operation and the activities, past and future necessary for its development

Preliminary surface charging analysis of Ariel payload dielectrics in early transfer orbit and L2-relevant space environment

Ariel [1] is the M4 mission of the ESA’s Cosmic Vision Program 2015-2025, whose aim is to characterize by lowresolution transit spectroscopy the atmospheres of over one thousand warm and hot exoplanets orbiting nearby stars. The operational orbit of the spacecraft is baselined as a large amplitude halo orbit around the Sun-Earth L2 Lagrangian point, as it offers the possibility of long uninterrupted observations in a fairly stable radiative and thermo-mechanical environment. A direct escape injection with a single passage through the Earth radiation belts and no eclipses is foreseen. The space environment around Earth and L2 presents significant design challenges to all spacecraft, including the effects of interactions with Sun radiation and charged particles owning to the surrounding plasma environment, potentially leading to dielectrics charging and unwanted electrostatic discharge (ESD) phenomena endangering the Payload operations and its data integrity. Here, we present some preliminary simulations and analyses about the Ariel Payload dielectrics and semiconductors charging along the transfer orbit from launch to L2 include

The instrument control unit of the ARIEL payload: design evolution following the unit and payload subsystems SRR (system requirements review)

ARIEL (Atmospheric Remote-sensing InfraRed Large-survey) is a medium-class mission of the European Space Agency, part of the Cosmic Vision program, whose launch is foreseen by early 2029. ARIEL aims to study the composition of exoplanet atmospheres, their formation and evolution. The ARIEL’s target will be a sample of about 1000 planets observed with one or more of the following methods: transit, eclipse and phase-curve spectroscopy, at both visible and infrared wavelengths simultaneously. The scientific payload is composed by a reflective telescope having a 1m-class elliptical primary mirror, built in solid Aluminium, and two focal-plane instruments: FGS and AIRS. FGS (Fine Guidance System)1 has the double purpose, as suggested by its name, of performing photometry (0.50-0.55 µm) and low resolution spectrometry over three bands (from 0.8 to 1.95 µm) and, simultaneously, to provide data to the spacecraft AOCS (Attitude and Orbit Control System) with a cadence of 10 Hz and contributing to reach a 0.02 arcsec pointing accuracy for bright targets. AIRS (ARIEL InfraRed Spectrometer) instrument will perform IR spectrometry in two wavelength ranges: between 1.95 and 3.9 µm (with a spectral resolution R > 100) and between 3.9 and 7.8 µm with a spectral resolution R > 30. This paper provides the status of the ICU (Instrument Control Unit), an electronic box whose purpose is to command and supply power to AIRS (as well as acquire science data from its two channels) and to command and control the TCU (Telescope Control Unit)

Legume Proteins and Peptides as Compounds in Nutraceuticals: A Structural Basis for Dietary Health Effects

In the current climate of food security, quality aspects of legume crops have primary market economic and health impact. Legume proteins and peptides have been discovered to have a role far beyond supplying amino acids for growth and maintenance of body tissues. Several proteins (enzymatic inhibitors, lectins, storage globulins) and peptides derived from them (lunasin, hydrophobic peptides) have shown anticarcinogenic, hypocholesterolemic, glucose-lowering, antioxidant, antimicrobial, and immunostimulant properties. Further understanding of how structural features of legume proteins affect in vivo digestion and production of bioactive sequences represents a key step in the valorization of nutraceutical potentiality of legume proteins and peptides derived from them. In this work, the relationship between structure and bioavailability of protein and peptides are reviewed and discussed

Hydrogen-Deuterium exchange kinetics in β-lactoglobulin (-)-epicatechin complexes studied by FTIR spectroscopy

Hydrogen-Deuterium exchange kinetics of β-lactoglobulin and β-lactoglobulin (-)-epicatechin solutions has been investigated through the analysis of the amide I absorption band at 1650cm(-1) in the FTIR spectrum. H-D substitution in NH amides and residues of the protein results in a slight red-shift and in intensity changes of the amide I components: either these effects have been inspected in the framework of the Principal Components Analysis methods. The present analysis allowed to unveil three H-D kinetics at the timescale of the oligomeric fluctuations of the protein. A fast mechanism (lifetime from 5 to 10min) can be ascribed to the dynamics of protein oligomers and aggregates at the scale of the quaternary structure variations, and it is not observed in the complexes β-lactoglobulin (-)-epicatechin. The other slowest kinetics, whose lifetimes are in the range 1-10h, are here associated to dynamics of high-molecular weight complexes that hamper the proton exchange. The role of (-)-epicatechin as an enhancer of the formation of stable high-molecular weight aggregates from β-lactoglobulin is also discussed by comparison of the lifetimes at different protein concentrations

Application of Fourier transform infrared spectroscopy to legume seed flour analysis

The secondary structure of legume (Phaseolus vulgaris L. and Lens culinaris L.) proteins was investigated by studying the amide I infrared absorption band in whole seed flours, before and after dry heating and autoclaving thermal treatments. The analysis procedure, set up on 7S and different model proteins, shows that the content of β-sheet structures in lentil is higher than in common bean (47% vs. 32%). The dry heating does not appreciably affect secondary structures in lentil, while it causes a reduction of β-sheets (to 13%), an increase of aggregates, and the appearance of random coil structures in common bean. The autoclaving treatment produces high amounts of aggregates in both legumes. However, in lentil, random coil structures are lower than in common bean and some β-sheet structures are still detectable. These results indicate that multimeric heat-induced complexes of legume proteins have a high stability because of the high content in β-sheet structures, in particular in lentil, which may adversely affect protein utilization. © 2007 Elsevier Ltd. All rights reserved

Epicatechin-induced conformational changes in β-lactoglobulin B monitored by FT-IR spectroscopy

The interaction between whey carrier protein β-lactoglobulin B and (-)-epicatechin, a major dietary flavonoid with a wide range of health-promoting biological activities, was investigated by Fourier transform infrared spectroscopy in physiological conditions. Amide I spectra of epicatechin - β-lactoglobulin complexes, in D2O buffer solutions, pD= 6.8, at molar ratios from 0.5:1 to 15:1, were measured by using a cell device specifically created. Changes in secondary structure elements at increasing epicatechin concentrations were quantified. Two different trends were observed for the intensities of β-sheet, random coil, and side chain contributions. At molar ratios ≤ 2 the β-exposed strand contributions (1625 cm-1) increased at the expence of the β-antiparallel sheet band (1637 cm-1). At molar ratios > 2 the intensities of both β structures slightly decreased. The same behaviour was observed for the side chain contributions (band around 1610 ÷ 1620 cm-1). In addition, a conformational transition to a slightly opened structure, followed by aggregate formation at the highest molar ratios, were revealed. The results suggest that binding of epicatechin to β-lactoglobulin in physiological conditions occurs at the surface of the protein molecule, resulting in protein dissociation at molar ratios ≤ 2 with minor changes in secondary structure. This finding provides further evidence for the possibility of successful use of the protein as a carrier of flavonoids, epicatechin included. © 2013 Nucara et al.; licensee Springer