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This paper reports on an experimental study of the influence of a nanosecond repetitively pulsed spark discharge on the stability domain of a propane/air flame. This flame is produced in a lean premixed swirled combustor representative of an aeronautical combustion chamber. The lean extinction limits of the flame produced without and with plasma are determined and compared. It appears that only a low mean discharge power is necessary to increase the flame stability domain. Lastly, the effects of several parameters (pulse repetition frequency, global flowrate, electrode location) are studied.

This paper reports on an experimental study of the influence of a nanosecond repetitively pulsed spark discharge on the stability domain of a propane/air flame. This flame is produced in a lean premixed swirled combustor representative of an aeronautical combustion chamber. The lean extinction limits of the flame produced without and with plasma are determined and compared. It appears that only a low mean discharge power is necessary to increase the flame stability domain. Lastly, the effects of several parameters (pulse repetition frequency, global flowrate, electrode location) are studied.

This chapter explores dynamics of lean premixed systems using large eddy simulation. Lean premixed prevaporized (LPP) injection systems are designed to offer a minimum NOx and soot emissions. The basic principle of LPP systems is to optimize combustion through an efficient mixing of fuel and air. This is achieved by vaporizing the initially liquid fuel and then mixing it with the air before combustion using for example a swirling flow. It is known that premixed combustion reduces pollutant emissions more than non-premixed combustion. Moreover, a lean mixture allows controlling the flame temperature and then NOx production because it increases with temperature. However, LPP systems are known to be very sensitive to couplings leading to many kind of unstable behaviors. This chapter helps in understanding the dynamical phenomena occurring in a LPP combustor, using advanced laser diagnostics. This chapter provides an experimental and numerical study of a Laboratory-scale gas turbine combustion chamber designed and operated at laboratoire EM2C. The results are compared with large eddy simulations performed at CERFACS.

Large Eddy Simulations of liquid O2/gaseous H2 coaxial flames at subcritical pressure conditions are reported in this paper. These simulations reproduce the experimental Mascotte cases A1, A10 and A30, operating at 1, 10 and 30 bar, respectively, and for which temperature measurements and experimental visualisations are available. The main objective of this work is to assess the accuracy of the multi-fluid Homogeneous Equilibrium Model (HEM) described in Pelletier et al. (Computers & Fluids, 2020) for rocket engine applications. Of particular interest is the comparison with the experimental temperature measurements from Grisch et al. (Aerospace science and technology, 2003). To that purpose, numerical simulations are conducted with care, in order to ensure a proper statistical convergence and estimate the influence of the grid resolution for each case. Despite the crude assumptions—no surface tension and no atomisation model, for instance—that are made with the HEM used in this work, results are found to be in reasonable agreements with the measurements for case A10, even with the coarser grid. For case A30, a fine mesh resolution is required to capture the low intensity recirculation zone downstream of the inner jet necessary to reproduce the shape of the experimental profile. Finally, case A1 simulations, with the lowest Weber number, show large departures with the experimental measurements. This is expected to be due to a deficiency of the model to properly reproduce the two-phase dispersed flow.

Quantifying the oscillation amplitude of thermoacoustic instabilities remains a critical and challenging issue, as it is a complex balance between driving and damping processes. The New Pressurized Coupled Cavities (NPCCs) setup designed for the study of acoustic damping is analyzed in this work. It is a cold-flow test rig mimicking the geometry of a liquid rocket engine and equipped with an acoustic forcing device. The chamber 1T mode triggers a strong non-linear harmonic response, while the 1T1L and 1T2L exhibit weak non-linearities. Disturbance energy budgets are used in large-eddy simulations to characterize the damping phenomena with the 1T2L and 1T1L forcing. The correct global damping of the system is retrieved, and local damping contributions are extracted. Then, a non-linear term representing the energy transfer to the harmonics is derived from non-linear acoustics theory. Combined with a linear model, this model correctly retrieves the limit-cycle of the 1T mode.

Molecular interactions are contingent upon the system’s dimensionality. Notably, comprehending the impact of dimensionality on protein–protein interactions holds paramount importance in foreseeing protein behaviour across diverse scenarios, encompassing both solution and membrane environments. Here, we unravel interactions among membrane proteins across various dimensionalities by quantifying their binding rates through fluorescence recovery experiments. Our findings are presented through the examination of two protein systems: streptavidin–biotin and a protein complex constituting a bacterial efflux pump. We present here an original approach for gauging a two-dimensional binding constant between membrane proteins embedded in two opposite membranes. The quotient of protein binding rates in solution and on the membrane represents a metric denoting the exploration distance of the interacting sites—a novel interpretation.

Matrix-assisted laser desorption ionization-time of flight mass spectrometry (MALDI-ToF MS) has been introduced in clinical routine microbiology laboratories. For the rapid diagnosis of urinary tract infections, culture-independent methods prior MALDI-mediated identification have been described. Here, we describe a comparison of three of these methods based on their performance of bacterial identification and their potential as a routine tool for microbiology labs : (i) differential centrifugation, (ii) urine filtration and (iii) a 5-h bacterial cultivation on solid culture media. For 19 urine samples, all methods were directly compared and correct bacterial species identification by MALDI was used as performance indicator. A higher percentage of correct MALDI identification was obtained after filtration (78.9 %) and the growth-based method (84.2 %) as compared to differential centrifugation (68.4 %). Additional testing of 76 mono-microbial specimens (bacteriuria > 10 5  CFU/mL) confirmed the good performance of short growth with a 90.8 % correct MALDI score, with a potentially better fit to the routine workflow of microbiology labs.

Tripartite efflux pumps are among the main actors responsible for antibiotics resistance in Gram-negative bacteria. In the last two decades, structural studies gave crucial information about the assembly interfaces and the mechanistic motions. Thus rigidifying the assembly seems to be an interesting way to hamper the drug efflux. In this context, xenon is a suitable probe for checking whether small ligands could act as conformational lockers by targeting hydrophobic cavities. Here we focus on OprN, the outer membrane channel of the MexEF efflux pump from Pseudomonas aeruginosa. After exposing OprN crystals to xenon gas pressure, 14 binding sites were observed using X-ray crystallography. These binding sites were unambiguously characterized in hydrophobic cavities of OprN. The major site is observed in the sensitive iris-like region gating the channel at the periplasmic side, built by the three key-residues Leu 405, Asp 109, and Arg 412. This arrangement defines along the tunnel axis a strong hydrophobic/polar gradient able to enhance the passive efflux mechanism of OprN. The other xenon atoms reveal strategic hydrophobic regions of the channel scaffold to target, with the aim to freeze the dynamic movements responsible of the open/close conformational equilibrium in OprN.

Membrane proteins are essential in the exchange processes of cells. In spite of great breakthrough in soluble proteins studies, membrane proteins structures, functions and interactions are still a challenge because of the difficulties related to their hydrophobic properties. Most of the experiments are performed with detergent-solubilized membrane proteins. However widely used micellar systems are far from the biological two-dimensions membrane. The development of new biomimetic membrane systems is fundamental to tackle this issue.We present an original approach that combines the Fluorescence Recovery After fringe Pattern Photobleaching technique and the use of a versatile sponge phase that makes it possible to extract crucial informations about interactions between membrane proteins embedded in the bilayers of a sponge phase. The clear advantage lies in the ability to adjust at will the spacing between two adjacent bilayers. When the membranes are far apart, the only possible interactions occur laterally between proteins embedded within the same bilayer, whereas when membranes get closer to each other, interactions between proteins embedded in facing membranes may occur as well.After validating our approach on the streptavidin-biotinylated peptide complex, we study the interactions between two membrane proteins, MexA and OprM, from a Pseudomonas aeruginosa efflux pump. The mode of interaction, the size of the protein complex and its potential stoichiometry are determined. In particular, we demonstrate that: MexA is effectively embedded in the bilayer; MexA and OprM do not interact laterally but can form a complex if they are embedded in opposite bilayers; the population of bound proteins is at its maximum for bilayers separated by a distance of about 200 A, which is the periplasmic thickness of Pseudomonas aeruginosa. We also show that the MexA-OprM association is enhanced when the position and orientation of the protein is restricted by the bilayers. We extract a stoichiometry for the complex that exhibits a strong pH dependance: from 2 to 6 MexA per OprM trimer when the pH decreases from 7.5 to 5.5.Our technique allows to study membrane protein associations in a membrane environment. It provides some challenging information about complexes such as geometry and stoichiometry.