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M 140

M 140 is a Meshing Technique used in computational fluid dynamics and finite element analysis.
It involves the division of a continuous domain into a set of discrete subdomains, known as elements, to facilitate the numerical solution of partial differential equations.
This process enhances the accuracy and reliability of simulations by capturing the complex geometry and physics of the problem.
The M 140 method is particularly useful for modeling intricate shapes, fluid-structure interactions, and multiphysics problems across a wide range of engineering and scientific disciplines.
Its versatility and computational efficiency make it an indispensible tool for researchers and engineers seeking to enhance the reproducibility and accuracy of their work.

Most cited protocols related to «M 140»

Arabidopsis thaliana wild-type (ecotype Columbia) and mutant plants were grown in soil supplemented with Hoagland medium in growth chambers under long-day conditions (16 h light/8 h darkness) at 22 °C during the day and 20 °C during the night. The light intensity was set at 140 μE m−2 s−1. The 2-Cys Prx A–2-Cys Prx B double mutant, denoted Δ2cp, was obtained by manual crossing of the single mutants 2cpA, line SALK_065264, and 2cpB, line SALK_017213, previously characterized (Kirchsteiger et al., 2009 (link)). Seeds resulting from this cross were checked for heterozygosity of T-DNA insertions in the 2cpA and 2cpB genes. The plants were then selfed and double homozygous plants were detected in the progeny by PCR analysis of genomic DNA using oligonucleotides a (5′-GAGAAGTTGAACACCGA-3′) and b (5′-GGGGACAAAGTGAGAATC-3′) for the 2cpA gene, and a′ (5′-CCACCTGAACCAAGAAAG-3′) and b′ (5′-CCTGCAAGACAACATCAC-3′) for the 2cpB gene in conjunction with the oligonucleotide T (5′-TGGTTCACGTAGTGGGCCATCG-3′) located in the T-DNA. A T-DNA homozygous line SALK_128914 (Alonso et al., 2003 (link)) in the single gene encoding Trx x of Arabidopsis (At1g50320 locus) was selected by PCR analysis of genomic DNA with oligonucleotides c (5′-GCCATGGACTCTATCGTCTC-3′) and d (5′-CCTTCCCTTCTGCTCCCT-3′) in conjunction with the T oligonucleotide. The NTRC knock-out mutant was described previously (Serrato et al., 2004 (link)).
Publication 2010
Arabidopsis Arabidopsis thalianas Culture Media Darkness DNA, A-Form Ecotype Genes Genome Heterozygote Homozygote Insertion Mutation Light M 140 Oligonucleotides Plant Embryos Plants
An aliquot of total lipid extract was analyzed with a Micromass Quattro Ultima triple quadrupole mass spectrometer equipped with a nanoelectrospray source. Samples were loaded into thin-wall nanoflow capillary tips (Waters) and analyzed by ESI-MS-MS in both positive (for phosphatidylcholine (PC), sphingomyelin (SM), phosphatidylserine (PS) and phosphatidylethanolamine (PE)), and negative ion mode (for PI, phosphatidylglycerol (PG), phosphatidic acid (PA), PS and PE). Capillary/cone voltages were 0·7 kV/50 V and 0·9 kV/50 V for positive ion and negative ion modes, respectively. Tandem mass spectra (MS-MS) were obtained using argon as the collision gas (~3·0 mTorr) with collision offset energies as follows: 35 V, PC in positive ion mode; 25 V, PE in positive ion mode; 22 V, PS in positive ion mode; 50 V, PE in negative ion mode; 28 V, PS in negative ion mode; 45 V, PI in negative ion mode; and 50 V, all glycerophospholipids detected by precursor scanning for m/z 153 in negative ion mode. MS-MS daughter ion scanning was performed with a collision-offset energy of 35 V. In positive ion mode, ions in the PC, PE, and PS spectra were annotated based on their [M+H-NMe3]+ for PC, and the corresponding fragment ions [M-140] and [PA-H] daughter ions for PE and PS respectively, and compared with that of their theoretical values. In negative ion mode, PL class peaks were assigned according to their [lyso-H], [lyso-H20-H], [lysoPA-H], or [lysoPA-H20-H] daughter ion derivatives. FAs were assigned based on their [M−H] values. Saturated and unsaturated FAs were assumed to be esterified to the sn-1 and sn-2 position of PLs, respectively. Each spectrum (600–1000 m/z) encompasses at least 50 repetitive scans, each of 4 s duration. Spectra were normally processed by subtraction of background and smoothed using Micronass processing algorithms unless otherwise indicated. The internal standards were used to ensure efficient ionization and fragmentation and as a control for sample variability.
Publication 2010
1-naphthol-8-amino-3,6-disulfonic acid Argon Capillaries Daughter derivatives Glycerophospholipids Lipids M 140 Mass Spectrometry Phosphatidic Acid Phosphatidylcholines phosphatidylethanolamine Phosphatidyl Glycerol Phosphatidylserines Phospholipids Radionuclide Imaging Retinal Cone Spectrometry, Mass, Electrospray Ionization Sphingomyelins Tandem Mass Spectrometry
The IgG3 (glyco)peptides were analyzed with nanoLC-reversed phase (RP)-electrospray (ESI)-ion trap (IT)-MS(/MS) on an Ultimate 3000 RSLCnano system (Dionex/Thermo Scientific) coupled to an amaZon speed ESI-IT-MS (Bruker Daltonics, Bremen, Germany). A precolumn (Acclaim PepMap C18 capillary column, 300 μm x 5 mm, particle size 5 μm, Dionex/Thermo Scientific) was used to wash and concentrate the sample, and separation was achieved on an Acclaim PepMap RSLC C18 nanocolumn (75 μm x 150 mm, particle size 2 μm, Dionex/Thermo Scientific) with a flow rate of 500 nl/min. The following linear gradient was used, with solvent A consisting of 0.1% formic acid in water and solvent B of 95% acetonitrile, 5% water: t = 0 min, 1% solvent B; t = 5 min, 1% B; t = 20 min, 25% B; t = 25 min, 70% B; t = 30 min, 70% B; t = 31 min, 1% B; t = 55 min, 1% B. The sample was ionized in positive ion mode with an ESI-nanosprayer (4500 V) using a bare fused silica capillary (internal diameter of 20 μm). The solvent was evaporated at 180 °C with a nitrogen flow of 5 liters/min. A CaptiveSpray nanoBooster (Bruker Daltonics) was mounted onto the mass spectrometer and saturated the nitrogen flow with ACN to enhance the sensitivity. The MS1 ion detection window was set at m/z 350–1400, and the MS2 window at m/z 140–2200. The three highest nonsingly charged peaks in each MS1 spectrum were automatically fragmented through collision-induced dissociation (CID). In order to identify the peptide sequence of proteinase K- and trypsin-generated O-glycopeptides, MS3 analysis was performed on manually selected precursors: the MS2 peak representing the peptide without sugars attached was targeted for fragmentation. In a separate LC-MS run, electron transfer dissociation fragmentation was done on selected precursor ions.
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Publication 2015
acetonitrile Capillaries Electron Transport Endopeptidase K formic acid Glycopeptides Hypersensitivity IgG3 Ions M 140 Nitrogen Peptides Silicon Dioxide Solvents Sugars Tandem Mass Spectrometry Trypsin Z 350
Prototype Satellite Relay Data-Loggers (SRDLs, Sea Mammal Research Unit, University of St Andrews, Scotland) were attached to six adult female bearded seals (August 2011 N = 4; August 2012 N = 2) and 10 adult female ringed seals (August 2012 only), in Svalbard Norway. Programming details for telemetry devices are outlined in Supplementary Materials. All research activities including both animal care and field site permitting during this study were approved and carried out under permits from the Norwegian Animal Care Authority (Forsøksdyrutvalget ref. 2010/45416 and 2011/42085) and the Governor of Svalbard (Sysselmannen på Svalbard Ref. 2011/00488-52). In addition to the standard sensors for measuring dive data, each SRDL contained an Argos-linked Fastloc GPS transmitter. All tags were programmed to the same specifications (S1 File), and the default speed parameter was used for the Argos Kalman filtering process (10ms-1). We are unaware of any other speed parameter setting being used in the marine mammal research community, and can thus not comment on the effects of varying this threshold with respect to the outcome of the Argos SRUKF process. Capturing and handling of these animals was conducted using the same methods as those outlined in [21 (link)]. Argos locations are derived as a by-product of all messages transmitted from the SRDL to the satellite system, while transmitted GPS data consist of a random subset of locations collected by the Fastloc GPS receiver on the animal, resulting in temporally decoupled Argos and GPS positions. Calibration studies of Fastloc GPS data show errors (at the 95th percentile level) between 24.2 m and 140 m for locations estimated by eight and five satellite acquisitions, respectively [22 ]. We removed all GPS locations with less than five satellite acquisitions, and henceforth assume the remaining GPS locations reflect the true position of the animal [23 (link)].
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Publication 2015
Animals M 140 Mammals Marines Medical Devices Phocidae Telemetry Woman
All mutants used are in the Columbia (Col) wild-type accession of Arabidopsis thaliana. The ddm1-2 allele was described before [33] (link). A new lhp1 allele, lhp1-6, was identified in the SALK T-DNA insertion mutant collection (SALK_011762). LHP1 and lhp1-7 cDNAs were cloned into vector pK7FWG2 [34] (link), which was used to transform plants by floral dip with Agrobacterium tumefaciens (strain GV3101). Seeds were germinated on sterile basal salts Murashige and Skoog (MS) medium (Duchefa, Brussels, Belgium), and plants were analyzed on plates or transferred to soil 10 days after germination. Alternatively, seeds were directly sown on soil. Plants were kept in Conviron growth chambers with mixed cold fluorescent and incandescent light (110 to 140 µmol m−2 s−1, 21±2°C) under long day (LD, 16h light) or short day (SD, 8h light) photoperiods or were alternatively raised in green houses.
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Publication 2009
Agrobacterium tumefaciens Alleles Arabidopsis thalianas Cloning Vectors Cold Temperature DNA, Complementary Germination Incandescence Light like heterochromatin protein 1 M 140 Plant Embryos Plants Salts Sterility, Reproductive Strains

Most recents protocols related to «M 140»

The unicellular green alga C. reinhardtii strain CC-125 cells (1.5 × 106) were cultured in 50 mL liquid tris-acetate-phosphate (TAP) media in 250 mL flasks (Harris, 1989 ) by shaking at 25°C and 140 rpm under constant white light of 90–100 μmol photons m−2 s−1. In addition to the wild type (WT), two transgenic C. reinhardtii lines (AtTHI-OE1 and AtTHI-OE2) harboring the Arabidopsis thaliana Thionin 2.1 gene, which encodes antibacterial peptides, thionins, were used to investigate genotype-dependent radiation-sensitivity. Cells were harvested at 800 × g, dispensed, and subjected to X- or γ-irradiation as described below. The subsequent post-irradiation cultivations of the cells were performed in 10 mL fresh TAP media in 50 mL conical tubes, with an initial optical density of 0.05 at 750 nm for mock (or control) under the same culture conditions. The basal TAP medium was supplemented with 5 or 10 mM NaHCO3 to evaluate the synergistic effect of X-rays and sodium bicarbonate on cell growth.
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Publication 2023
Acetate Animals, Transgenic Anti-Bacterial Agents Arabidopsis thalianas Bicarbonate, Sodium Cells G-800 Genes Genotype Light M 140 Peptides Phosphates Radiation Tolerance Radiotherapy Strains Thionins Tromethamine X-Rays, Diagnostic
Colloidal silica nanoparticles
of an average diameter of 50 nm were purchased from Nissan Inc. Two
types of nanoparticles were prepared: (1) particles with grafted PMMA
with a graft density of 0.34 chains/nm2 and a molecular
weight of 120 000 g/mol, (2) particles with grafted polyaniline
acrylate polymer at a graft density of 0.34 chains/nm2 and
a molecular weight of 134 000 g/mol.
To create the grafted
polymers, poly(methyl methacrylate) (PMMA) and poly(acrylic acid N-hyroxysuccinimide) (PNAS) were synthesized by surface-initiated
reversible addition-fragmentation chain transfer polymerization (SI-RAFT).
The RAFT agent was 2-(dodecylthiocarbonothioylthio) propanoic acid
(DoPAT). All chemicals were used as received unless otherwise specified.
Methyl methacrylate (MMA, 99%, Acros) was purified by filtration through
an activated basic alumina column. Azobisisobutyronitrile (AIBN) was
recrystallized from methanol before use. Molecular weights and dispersity
were determined by monitoring monomer conversion through 1H NMR and gel permeation chromatography (GPC). THF was used as the
eluent for GPC at 30 °C and a flow rate of 1.0 mL/min. GPC was
calibrated with poly(methyl methacrylate) (PMMA) standards obtained
from Polymer Laboratories.
To synthesize free polyaniline acrylate,
DoPAT (5 mg, 0.014 mmol),
NAS (0.482 g, 2.84 mmol), and AIBN (140 μL in 0.01 M solution)
were dispersed in 4.75 mL of DMF and transferred into a dried Schlenk
flask. The mixture was degassed by three freeze–pump–thaw
cycles, back-filled with nitrogen, and then placed in an oil bath
at 65 °C. The polymerization solution was quenched in an ice
bath and exposed to air after 24 h. The polymer solution was precipitated
into diethyl ether and centrifuged at 6000 rpm for 5 min. The dispersion-precipitation
process was repeated four times. The polymer was then redissolved
in 5 mL of DMF and sparged with nitrogen for 15 min. N-Phenyl-p-phenylenediamine (1.05 g, 5.6 mmol) was
dissolved in 2 mL of DMF. The solution was then added to the polymer
solution where it was then transferred to an oil bath at 110 °C
for 24 h. The polymerization was quenched in an ice bath and precipitated
into diethyl ether and centrifuged at 6000 rpm for 5 min. The polymer
was then dissolved in THF, and the dispersion-precipitation process
was repeated until the supernatant was colorless. Polyaniline-acrylate-grafted
NPs were synthesized by a surface-initiated reversible addition-fragmentation
chain transfer polymerization (SI-RAFT).15 (link) A typical polyaniline-acrylate-grafted NP synthesis was: DoPAT-NP
(0.05 g, σ = 0.34 chains/nm2), NAS (0.30 g, 1.77
mmol), and AIBN (18 μL in a 0.1 M solution) were dispersed in
5 mL of DMF and transferred to a Schlenk flask. The remaining procedure
is identical to the free polyaniline acrylate synthesis.
Publication 2023
1H NMR 4-aminodiphenylamine acrylate Anabolism azobis(isobutyronitrile) Bath Ethyl Ether Filtration Freezing Gel Chromatography M 140 Methanol Methylmethacrylate Nitrogen Oxide, Aluminum Peptide Nucleic Acids polyacrylic acid polyaniline Polymerization Polymers Polymethyl Methacrylate propionic acid Silicon Dioxide
Using time-dependent two-phase flow physics, the finite element simulations of a 2D droplet on a moving plate are performed in COMSOL Multiphysics 5.6. Navier-Stokes equations are solved in the liquid and air domain. Liquid/air/solid interfaces are modeled using the level-set method. Before prescribing the motion to the plate, the droplet is allowed to equilibrate on the stationary plate to achieve its equilibrium shape based on the prescribed contact angle. Following equilibration, the plate is prescribed a sinusoidal displacement using a moving mesh interface, where it is modeled as a moving boundary within a deforming domain. Automatic remeshing of the domain is performed at specified timesteps to prevent excessive deformation of the mesh elements because of the moving boundary. For the outer boundaries of the domain, we prescribed the outlet boundary condition, specifying the static pressure to zero. For the wetted wall, i.e., the surface of the plate, we defined a static contact angle with a Navier-slip equal to the maximum size of the mesh element. We used a free triangular mesh with a maximum element size of 0.015 mm and a minimum of 0.0001 mm. The reinitialization parameter for the level set method is set to 0.5 m/s, and the parameter controlling interface thickness is equal to the mesh element’s maximum size. We simulated droplets at different contact angles ranging from 100–180. For 2D simulations, we fixed the area of the droplet corresponding to the droplet’s diameter of 1 mm, forming a perfect circle and using this same area to equilibrate droplets under gravity at different contact angles. Given no coupling between the upper and lower springs (Supplementary Information, Section II, B), we prescribed the sinusoidal motion to the plate of the form z=Asin(2πfstπ/2) where f is the frequency of plate at a constant peak acceleration of 140 m/s2 with the frequencies of vibration ranging from 50 Hz to 300 Hz. We have also performed simulations for droplet sizes 1.2 mm and 1.4 mm, and for acceleration 80 m/s2 which show good match with the drop-on-plate experiments (Fig. 2 and Supplementary Fig. 10). However, we didn’t find significant differences between the superpropulsion curves when compared with a droplet of 1 mm size.
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Publication 2023
Acceleration Gravity M 140 Natural Springs Pressure Sinusoidal Beds Vibration
The Saccharomyces cerevisiae strains used are all BY4741 derivative and are listed in Table S1. To generate cdh1∆::HIS3 strain, cdh1∆::KanMX4 was transformed with a DNA fragment containing HIS3MX. To construct double mutant strains, the DNA fragment containing cdh1∆::HIS3 was amplified and transformed in the deletion strains. To generate Rpn4-HAcdh1Δ::kan strain, Rpn4-HA:HIS3 was transformed with a DNA fragment containing cdh1∆::KanMX4. Strains were transformed by the standard lithium acetate procedure [59 (link)]. Gene deletion was confirmed by PCR. For overexpression of Cdh1-m11 and Sod2p, cells were transformed with the plasmids pRS416-GALL-3HA-Cdh1-m11 [26 (link)] and Yep352-SOD2 [45 (link)], respectively.
Cells were grown in rich medium [YPGal: 2% (w/v) galactose, 1% (w/v) yeast extract, 2% (w/v) bactopeptone] or synthetic complete medium [SC: 0.67% (w/v) Bacto-yeast nitrogen base w/o amino acids, 2% (w/v) glucose and 0.2% (w/v) Dropout mix] lacking uracil/leucine, as appropriate. For Cdh1-m11 overexpression, cells were grown in YPRaff medium [2% (w/v) raffinose, 1% (w/v) yeast extract, 2% (w/v) bactopeptone] overnight until mid-log phase and cultured with 4% galactose for 3h before oxygen consumption analysis. Cultures were routinely grown at 26 °C in an orbital shaker at 140 r.p.m.
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Publication 2023
Amino Acids, Basic Bacto-peptone CDH1 protein, human Cells Deletion Mutation Galactose Gene Deletion Glucose Leucine lithium acetate M 140 Nitrogen Oxygen Consumption Plasmids Raffinose Saccharomyces cerevisiae SOD2 protein, human Strains Uracil
Pilot-scale cultures were carried out in three identical single-use ‘hanging-bag’ (HB) photobioreactors (PBR) [29 (link)]. Each PBR was made from heat-sealed polythene layflat tubing (1000-gauge, UK packing, London, UK) with a width of 10.2 cm and a final working volume of 5 L. A late logarithmic-phase culture was used to inoculate the HBs to an initial optical density (OD) reading of 0.015 at 750 nm. The cells were grown in a temperature-controlled room at 24.5 °C under constant illumination provided by three light-emitting diode (LED) panels with an average light intensity of 140 µmol.m−2.s−1. The cultures were aerated and recirculated using a constant air flowrate of 1 L/min. No carbon dioxide was supplemented. The growth was monitored by off-line OD750 readings using semi-micro acrylic cuvettes with a path length of 10 mm and fresh TAP medium as blank.
The cultures were harvested after 3 days upon reaching the end of the logarithmic phase. Before harvesting, each HB was sampled for dry cell weight (DCW) measurements and immunoblotting (biological triplicates). The pellets for DCW were obtained from 50 mL samples after centrifugation (5000 g, 10 min, 12 °C) and stored at –20 °C for future freeze drying. For immunoblotting, 10 mL samples were centrifuged as previously described, snap-frozen in liquid nitrogen and stored at –80 °C for later analyses.
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Publication 2023
Biopharmaceuticals Carbon dioxide Centrifugation Freezing Light Lighting M 140 Nitrogen Pellets, Drug Photobioreactors Polyethylene

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More about "M 140"

Mesh technique, computational fluid dynamics, finite element analysis, numerical simulation, partial differential equations, complex geometry, fluid-structure interactions, multiphysics problems, engineering, scientific research, reproducibility, accuracy, Q Exactive Plus, Acclaim PepMap 100 C18 column, QIAGEN QIAamp®DNA blood mini and midi kits, Q Exactive Orbitrap, Brucella Broth media, FlexImaging 4.1, PepMap C18, Nucleoside Digestion Mix, 6490A Triple Quadrupole Mass Detector, XSelect HSS T3 XP column.
The M 140 meshing technique is a powerful tool used in computational fluid dynamics and finite element analysis to enhance the accuracy and reliability of numerical simulations.
By dividing a continuous domain into discrete subdomains, known as elements, the M 140 method can effectively capture the complex geometry and physics of a problem, enabling researchers and engineers to model intricate shapes, fluid-structure interactions, and multiphysics scenarios across a wide range of disciplines.
This versatile and computationally efficient approach is indispensible for improving the reproducibility and accuracy of scientific research and engineering applications, making it a crucial component in workflows that leverage advanced analytical technologies like the Q Exactive Plus, Acclaim PepMap 100 C18 column, QIAGEN QIAamp®DNA blood mini and midi kits, Q Exactive Orbitrap, Brucella Broth media, FlexImaging 4.1, PepMap C18, Nucleoside Digestion Mix, 6490A Triple Quadrupole Mass Detector, and XSelect HSS T3 XP column.