Sensitivity of a Bolometric Interferometer to the CMB power spectrum

Context. The search for B-mode polarization fluctuations in the Cosmic Microwave Background is one of the main challenges of modern cosmology. The expected level of the B-mode signal is very low and therefore requires the development of highly sensitive instruments with low systematic errors. An appealing possibility is bolometric interferometry. Aims. We compare in this article the sensitivity on the CMB angular power spectrum achieved with direct imaging, heterodyne and bolometric interferometry. Methods. Using a simple power spectrum estimator, we calculate its variance leading to the counterpart for bolometric interferometry of the well known Knox formula for direct imaging. Results. We find that bolometric interferometry is less sensitive than direct imaging. However, as expected, it is finally more sensitive than heterodyne interferometry due to the low noise of the bolometers. It therefore appears as an alternative to direct imagers with different and possibly lower systematic errors, mainly due to the absence of an optical setup in front of the horns.Comment: 5 pages, 3 figures. This last version matches the published version (Astronomy and Astrophysics 491 3 (2008) 923-927). Sensitivity of Heterodyne Interferometers modified by a factor of tw

Transport de protéines natives, partiellement et complètement dépliées à travers des nanopores protéiques et artificiels

Nous étudions le transport de protéines natives, partiellement ou complètement dépliées à travers des nanopores protéiques ou solides à l échelle de la molécule unique en utilisant une détection électrique. Le système modèle que nous avons choisi est la protéine MalE sauvage ou mutante, en particulier la protéine MalE 219 qui se déplie à de plus faibles concentrations d agent dénaturant que la protéine sauvage. Nous montrons que la translocation de protéines partiellement dépliées à travers un canal protéique, l hémolysine du staphylocoque doré, dépend des conformations individuelles que nous pouvons distinguer. Les molécules dépliées passent rapidement dans les nanopores. Nous mesurons directement leur fraction en fonction de la concentration en agent dénaturant. La technique est très sensible aux mutations affectant le repliement.. Nous avons également étudié le transport de protéines à travers des nanopores solides dans différents cas. Nous comparons d abord le transport de protéines natives et de protéines complètement dépliées à travers un nanopore de grand diamètre puis nous étudions la translocation de protéines dépliées à travers un nanopore étroit de diamètre inférieur à la taille de la protéine. Nous observons différents régimes de translocation quand nous varions le champ électrique appliqué que nous interprétons à l aide d un modèle théorique simple.We study the transport of native, partially or completely unfolded proteins through protein or solid-state nanopores at the single molecule level using an electrical detection. The model system that we use is the wild-type MalE or mutant protein, in particular MalE219, which unfolds at lower concentration of denaturing agent than the wild type. We show that the translocation of partially unfolded proteins through the Hemolysin protein channel, a toxin from Staphylococcus aureus, depends on of individual conformations that we can distinguish. The unfolded proteins pass rapidly through the nanopores. We directly measure their proportion as a function of the concentration of denaturing agent. The technique is very sensitive to the mutations affecting the folding properties. We also study the transport of proteins through solid-state nanopores in different situations. We first compare the transport of native and fully unfolded proteins through a nanopore of large diameter. We then study the tranlocation of unfolded proteins through a narrow pore, whose diameter is smaller than the protein size. We observe different regimes of translocation by varying the applied electric field, which we interpret using a simple theoretical model.EVRY-Bib. électronique (912289901) / SudocSudocFranceF

Thermostable virus portal proteins as reprogrammable adapters for solid-state nanopore sensors

Nanopore-based sensors are advancing the sensitivity and selectivity of single-molecule detection in molecular medicine and biotechnology. Current electrical sensing devices are based on either membrane protein pores supported in planar lipid bilayers or solid-state (SS) pores fabricated in thin metallic membranes. While both types of nanosensors have been used in a variety of applications, each has inherent disadvantages that limit its use. Hybrid nanopores, consisting of a protein pore supported within a SS membrane, combine the robust nature of SS membranes with the precise and simple engineering of protein nanopores. We demonstrate here a novel lipid-free hybrid nanopore comprising a natural DNA pore from a thermostable virus, electrokinetically inserted into a larger nanopore supported in a silicon nitride membrane. The hybrid pore is stable and easy to fabricate, and, most importantly, exhibits low peripheral leakage allowing sensing and discrimination among different types of biomolecules

Porphyrin-Assisted Docking of a Thermophage Portal Protein into Lipid Bilayers : Nanopore Engineering and Characterization

Nanopore-based sensors for nucleic acid sequencing and single-molecule detection typically employ pore-forming membrane proteins with hydrophobic external surfaces, suitable for insertion into a lipid bilayer. In contrast, hydrophilic pore-containing molecules, such as DNA origami, have been shown to require chemical modification to favor insertion into a lipid environment. In this work, we describe a strategy for inserting polar proteins with an inner pore into lipid membranes, focusing here on a circular 12-subunit assembly of the thermophage G20c portal protein. X-ray crystallography, electron microscopy, molecular dynamics, and thermal/chaotrope denaturation experiments all find the G20c portal protein to have a highly stable structure, favorable for nanopore sensing applications. Porphyrin conjugation to a cysteine mutant in the protein facilitates the protein's insertion into lipid bilayers, allowing us to probe ion transport through the pore. Finally, we probed the portal interior size and shape using a series of cyclodextrins of varying sizes, revealing asymmetric transport that possibly originates from the portal's DNA-ratchet function

Planck early results. VI. The High Frequency Instrument data processing

We describe the processing of the 336 billion raw data samples from the High Frequency Instrument (HFI) which we performed to produce six temperature maps from the first 295 days of Planck-HFI survey data. These maps provide an accurate rendition of the sky emission at 100, 143, 217, 353, 545 and 857GHz with an angular resolution ranging from 9.9 to 4.4 . The white noise level is around 1.5 μK degree or less in the 3 main CMB channels (100–217 GHz). The photometric accuracy is better than 2% at frequencies between 100 and 353 GHz and around 7% at the two highest frequencies. The maps created by the HFI Data Processing Centre reach our goals in terms of sensitivity, resolution, and photometric accuracy. They are already sufficiently accurate and well-characterised to allow scientific analyses which are presented in an accompanying series of early papers. At this stage, HFI data appears to be of high quality and we expect that with further refinements of the data processing we should be able to achieve, or exceed, the science goals of the Planck project

Planck early results: first assessment of the High Frequency Instrument in-flight performance

The Planck High Frequency Instrument (HFI) is designed to measure the temperature and polarization anisotropies of the Cosmic Microwave Background and galactic foregrounds in six wide bands centered at 100, 143, 217, 353, 545 and 857 GHz at an angular resolution of 10' (100 GHz), 7' (143 GHz), and 5' (217 GHz and higher). HFI has been operating flawlessly since launch on 14 May 2009. The bolometers cooled to 100 mK as planned. The settings of the readout electronics, such as the bolometer bias current, that optimize HFI's noise performance on orbit are nearly the same as the ones chosen during ground testing. Observations of Mars, Jupiter, and Saturn verified both the optical system and the time response of the detection chains. The optical beams are close to predictions from physical optics modeling. The time response of the detection chains is close to pre-launch measurements. The detectors suffer from an unexpected high flux of cosmic rays related to low solar activity. Due to the redundancy of Planck's observations strategy, the removal of a few percent of data contaminated by glitches does not affect significantly the sensitivity. The cosmic rays heat up significantly the bolometer plate and the modulation on periods of days to months of the heat load creates a common drift of all bolometer signals which do not affect the scientific capabilities. Only the high energy cosmic rays showers induce inhomogeneous heating which is a probable source of low frequency noise.Comment: Submitted to A&A. 22 pages, 6 tables, 21 figures. One of a set of simultaneous papers for the Planck Missio

Planck early results. VI. The High Frequency Instrument data processing

We describe the processing of the 336 billion raw data samples from the High Frequency Instrument (HFI) which we performed to produce six temperature maps from the first 295 days of Planck-HFI survey data. These maps provide an accurate rendition of the sky emission at 100, 143, 217, 353, 545 and 857 GHz with an angular resolution ranging from 9.9 to 4.4^2. The white noise level is around 1.5 {\mu}K degree or less in the 3 main CMB channels (100--217GHz). The photometric accuracy is better than 2% at frequencies between 100 and 353 GHz and around 7% at the two highest frequencies. The maps created by the HFI Data Processing Centre reach our goals in terms of sensitivity, resolution, and photometric accuracy. They are already sufficiently accurate and well-characterised to allow scientific analyses which are presented in an accompanying series of early papers. At this stage, HFI data appears to be of high quality and we expect that with further refinements of the data processing we should be able to achieve, or exceed, the science goals of the Planck project.Comment: Replaced by the accepted version for publication, as part of a package of papers describing first results of the Planck mission The paper with figures at full resolution and full color tables can also be downloaded from the ESA site http://www.rssd.esa.int/Planc

Transport of native, partially and completely unfolded proteins through protein and solid-state nanopores

Nous étudions le transport de protéines natives, partiellement ou complètement dépliées à travers des nanopores protéiques ou solides à l’échelle de la molécule unique en utilisant une détection électrique. Le système modèle que nous avons choisi est la protéine MalE sauvage ou mutante, en particulier la protéine MalE 219 qui se déplie à de plus faibles concentrations d’agent dénaturant que la protéine sauvage. Nous montrons que la translocation de protéines partiellement dépliées à travers un canal protéique, l’hémolysine du staphylocoque doré, dépend des conformations individuelles que nous pouvons distinguer. Les molécules dépliées passent rapidement dans les nanopores. Nous mesurons directement leur fraction en fonction de la concentration en agent dénaturant. La technique est très sensible aux mutations affectant le repliement.. Nous avons également étudié le transport de protéines à travers des nanopores solides dans différents cas. Nous comparons d’abord le transport de protéines natives et de protéines complètement dépliées à travers un nanopore de grand diamètre puis nous étudions la translocation de protéines dépliées à travers un nanopore étroit de diamètre inférieur à la taille de la protéine. Nous observons différents régimes de translocation quand nous varions le champ électrique appliqué que nous interprétons à l’aide d’un modèle théorique simple.We study the transport of native, partially or completely unfolded proteins through protein or solid-state nanopores at the single molecule level using an electrical detection. The model system that we use is the wild-type MalE or mutant protein, in particular MalE219, which unfolds at lower concentration of denaturing agent than the wild type. We show that the translocation of partially unfolded proteins through the Hemolysin protein channel, a toxin from Staphylococcus aureus, depends on of individual conformations that we can distinguish. The unfolded proteins pass rapidly through the nanopores. We directly measure their proportion as a function of the concentration of denaturing agent. The technique is very sensitive to the mutations affecting the folding properties. We also study the transport of proteins through solid-state nanopores in different situations. We first compare the transport of native and fully unfolded proteins through a nanopore of large diameter. We then study the tranlocation of unfolded proteins through a narrow pore, whose diameter is smaller than the protein size. We observe different regimes of translocation by varying the applied electric field, which we interpret using a simple theoretical model