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Dimyristoylphosphatidylcholine

Dimyristoylphosphatidylcholine is a phospholipid composed of two myristic acid chains attached to a glycerol backbone with a choline head group.
It is a common model compound used in research on cell membranes and lipid bilayer structures.
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Most cited protocols related to «Dimyristoylphosphatidylcholine»

To facilitate the building process of a membrane bilayer using the insertion and replacement methods, the library of lipid bilayers with holes and the library of lipid molecules have been generated. There are 90 pre-equilibrated lipid bilayers with a hole of radius from 1 Å to 45 Å for two different number of lipid molecules (128 or 256 lipid molecules) in the lipid library for DMPC, DPPC, and POPC. Starting from an equilibrated membrane bilayer of each type of lipid, the cylindrical pore has been generated by increasing the pore radius by 1 Å every 50 ps with a cylindrical harmonic restraint at 303.15 K (DMPC and POPC) and at 323.15 K (DPPC). The maximum number of lipid molecules available in each lipid bilayer is 256 (128 for each leaflet), and the largest bilayer size is 90 Å by 90 Å. The lipid molecule library for each type of lipid contains 2,000 different conformations. Lipid molecules are randomly selected from a 2.5 ns trajectory of each lipid bilayer. All the calculations were performed with CHARMM [28] , and the all-atom parameter set PARAM22 for proteins [29] including dihedral cross-term corrections (CMAP) [30] (link) and a modified TIP3P water model [31] , as well as recently optimized lipid parameters [32] .
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Publication 2007
cDNA Library Dimyristoylphosphatidylcholine Lipid Bilayers Lipids Proteins Radius Tissue, Membrane
We describe here application of the UniDec approach to problems of increasing complexity: membrane protein AqpZ; small heat shock proteins HSP17.7, HSP16.5, and αB-crystallin; and lipoprotein Nanodiscs.
MS and IM-MS data of aquaporin Z (AqpZ) with bound 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) obtained at 100 V accelerating potential into a dedicated collision cell was analyzed using UniDec by limiting the mass range to between 95 and 105 kDa.27 (link) An example of how the algorithm performs without mass limitations is shown in Figure S-2. Data was smoothed in MassLynx 4.1 software (Waters Corp.) before analysis with Transform and MaxEnt, which used the same mass limitation.
Deconvolution of subunit exchange data from HSP17.7 was performed by limiting the allowed mass range to between 211 kDa and 222 kDa. Tandem MS spectra of the isolated +47 charge state of HSP16.5 24-mers were summed across multiple collision voltages to compile an aggregate spectrum.28 (link) Deconvolution was performed by limiting the charge state between 10 and 49 and manually defining the +47 charge state, which was necessary because only one charge state was isolated in the MS/MS experiment. Collision induced dissociation (CID) spectra of αB-crystallin were obtained similarly. Masses were limited to within 3000 Da of a wide range of potential oligomer complexes ranging from 1 to 74 subunits of a 20085 Da monomer. Charge was limited to between 5 and 84. In addition to the charge-smooth filter, a mass-smooth filter was applied to smooth the distribution of dimer units.
Nanodiscs with 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) and POPC were analyzed with a linear drift cell Waters Synapt G1 ion mobility-mass spectrometer.29 (link) Data was deconvolved without a charge filter but by using a mass filter to smooth the distribution of lipids. Masses were limited to between 100 kDa and 175 kDa. Conversion from arrival time to collision cross section (CCS) was performed using the Mason-Schamp equation as described previously,27 (link),29 (link) using t0 values calibrated from alcohol dehydrogenase analyzed under the same instrumental conditions.
Publication 2015
Cells Crystallins Dehydrogenase, Alcohol Dimyristoylphosphatidylcholine Glycerylphosphorylcholine GPER protein, human Heat-Shock Proteins, Small Lipids Lipoproteins Phosphorylcholine plasma protein Z Protein Subunits Range of Motion, Articular Tandem Mass Spectrometry Tissue, Membrane Water Channel
All simulations were performed
in the isothermal–isobaric ensemble, NPT,
at a pressure of 1 atm. The pressure was held constant by using the
Parrinello–Rahman barostat77 with
a coupling constant of 10.0 ps with an isothermal compressibility
of 4.5 × 10–5 bar–1. For
the bulk liquids an isotropic pressure coupling was used and for the
bilayer simulations a semi-isotropic pressure coupling scheme was
used. The temperature was kept constant by the Nosé–Hoover
thermostat78 ,79 (link) with a coupling constant of 0.5 ps. The
lipid bilayer and water were coupled separately to the thermostat.
Long-range electrostatic interactions were treated by a particle-mesh
Ewald scheme80 ,81 with a real-space cutoff at 1.4
nm with a Fourier spacing of 0.10 nm and a fourth-order interpolation
to the Ewald mesh. Single-atom charge groups were used. van der Waals
interactions were truncated at 1.5 nm and treated with a switch function
from 1.4 nm. Long-range corrections for the potential and pressure
were added.51 The inclusion of long-range
corrections should eliminate the LJ cutoff dependency in the simulations.
Due to the fact that lipid bilayers are inhomogeneous systems the
method introduced by Lagüe et al.82 to add long-range corrections could be applied instead. Periodic
boundary conditions were imposed in every dimension. A time step of
2 fs was used with a Leap-Frog integrator. The LINCS algorithm83 was used to freeze all covalent bonds in the
lipid, and the analytical SETTLE84 method
was used to hold the bonds and angle in water constant. The TIP3P
water model85 was the water model of choice.
The choice of water model can be explained by the fact that TIP3P
is the default water model in major FFs such as AMBER and CHARMM and
since one of the aims of the work presented here was to create a lipid
FF compatible with AMBER this was a natural choice. Further, earlier
work of Högberg et al.31 (link) has shown
that there is flexibility in the choice of water model for AA simulations
of lipid bilayers. Atomic coordinates were saved every 1 ps and the
neighbor list was updated every 10th step.
Bulk liquids were
simulated with a simulation box consisting of 128 molecules for the
larger alkanes and 256 for the smaller alkanes (hexane and heptane)
at a temperature of 298.15 K. The lipid bilayer systems were prepared
using the CHARMM-GUI86 (link),87 (link) with 128 lipids in total, 64
in each leaflet. In order to achieve proper hydration, 30 TIP3P water
molecules were added per lipid. Three different lipid types were simulated,
DLPC (12:0/12:0), DMPC (14:0/14:0), and DPPC (16:0/16:0). These system
were investigated under a range of temperatures; see Table 1 for an overview of all simulations performed. All
lipid bilayer systems were equilibrated for 40 ns before production
runs were initiated which lasted for 300–500 ns. All MD simulations
were performed with the Gromacs88 software
package (versions 4.5.3 and 4.5.4). All analysis were made with the
analysis tools that come with the MDynaMix software package.89 System snapshots were rendered and analyzed
with VMD.90 Neutron scattering form factors
were computed with the SIMtoEXP software.91 (link)The calculations of free energies of solvation in
water and cyclohexane
were performed by using thermodynamic integration over 35 λ
values in the range between 0 and 1. A soft core potential (SCP) was
used to avoid singularities when the solute is almost decoupled from
the solvent. The α-parameters used for the SCP and the simulation
workflow were set following the methodology described by Sapay and
Tieleman.92 (link) The amino acid analogues were
solvated with 512 and 1536 molecules of cyclohexane and water, respectively.
Publication 2012
Alkanes Amber Amino Acids ARID1A protein, human Cyclohexane Dietary Fiber Dimyristoylphosphatidylcholine Electrostatics Freezing Heptane Lipid Bilayers Lipids Maritally Unattached n-hexane Natural Selection Pressure Rana Solvents
For the lipid tails hexadecane
was chosen as a model compound for computing the charges. It is well-known
that partial atomic charges are conformation dependent52 but previous FFs have been parametrized from optimized
geometries. In order to address this issue, we performed a 10 ns long
MD simulation with pure hexadecane with FF parameters earlier derived
by our group.31 (link) After the simulation, 54
random conformations were extracted and used for computing the charges
which were then averaged over all conformations in order to obtain
a final set. In this way, we obtained Boltzmann-averaged charges over
an ensemble of conformations in a procedure equivalent to the one
used by Sonne et al.30 (link) We hope that by
averaging over an ensemble of conformations the effects of the conformational
dependence of partial charges are minimized. In computation of atomic
charges, a dielectric constant of 2.04 was used to mimic the dielectric
environment of the membrane’s hydrophobic part.
Atomic
charges for the lipid head group were obtained in a similar fashion
where 26 random conformations were chosen from a 20 ns long simulation
of an equilibrated bilayer (DMPC) with the same FF parameters used
in the initial simulation of hexadecane. A large part of the hydrophobic
parts of the lipids were then cut off in order to save CPU time and
the cropped lipids were placed in dielectric continuum with ε
= 78.4 in order to mimic the aqueous environment. Inclusion of solvent
effects results in a FF with implicitly polarized charges optimized
for condensed phase simulations. This has been proven to give reliable
results without any performance loss.53 (link)For each molecular conformation, the charges were computed
using
the restricted electrostatic potential approach54 (RESP) with the DFT method using the B3LYP exchange-correlation
functional55 −58 and the cc-pVTZ basis set.59 The electrostatic
potential was sampled with the Merz–Singh–Kollman scheme60 by single-point calculations and fitted during
the two-stage procedure developed by Cornell et al.61 All solvent effects were modeled by placing the molecule
in a polarizable continuum with different dielectric constant (see
above) with the IEFPCM continuum solvent model.62 ,63 The quantum mechanical calculations were performed with the Gaussian09
software package,64 and the RESP calculations
were performed with the Red software.65 (link) In subsequent molecular dynamics simulations, Coulombic 1–4
interactions were scaled by a factor of 0.8333.
The way the
atomic charges have been calculated and used in MD
simulations makes them compatible with the AMBER03 FF53 (link) and since the charges in all AMBER FFs are derived from
the RESP the lipid FF presented here is compatible with most members
of the AMBER FF family. This is of importance since there is a growing
interest in simulating membrane proteins in their native environment19 (link),66 (link) and also peptide partitioning in biological membranes.67 (link),68 (link) Ongoing work aims to clarify which AMBER biomolecular FFs that work
sufficiently well together with the current parameters. A preliminary
test of the compatibility of the lipid parameters and the AMBER03
FF is presented further down.
Boltzmann averaging over charges
introduces temperature dependency
on the charges and in order to see the impact of temperature, simulations
with different temperatures (298, 303, 310, 318, and 325 K) were performed
with hexadecane using the methodology described above. No explicit
temperature dependence could be found over this range of temperatures,
making the charges reliable and robust with respect to temperature,
at least within the interval tested here (data not shown).
Publication 2012
Amber Biopharmaceuticals Dimyristoylphosphatidylcholine Electrostatics factor A Head hexadecane Lipid A Lipids Membrane Proteins Peptides Respiratory Rate Solvents Tail Tissue, Membrane
EmrE was expressed and purified using a 6× His-tag, which was then removed with thrombin. Purification was performed in decylmaltoside (DM) or dodecylmaltoside (DDM). EmrE was reconstituted into dimyristoylphosphatidylcholine (DMPC) or dilauroylphosphatidylcholine (DLPC) liposomes using standard methods and then formed into isotropic bicelles by addition of dihexanoylphosphatidylcholine (DHPC) and several freeze-thaw cycles. Protein concentration was determined using absorbance at 280 nm, with an extinction coefficient determined by amino acid analysis. ITC was performed by titrating 54 μM TPP+ stock solutions into 10 μM EmrE, with matching concentrations of detergent or lipid in both solutions.
Bulk FRET labeling was performed in liposomes to separately label residues on either side of the membrane. An “antiparallel” sample was labeled with donor and acceptor on opposite sides and a “parallel” sample was labeled with donor and acceptor on the same side. Donor-only and acceptor-only controls were labeled with dye only on the exterior of the liposome, reconstituted into bicelles and then mixed. Single-molecule FRET samples were labeled in micelles and experiments were performed using a wide-field total internal reflection fluorescence microscope (TIRF) setup43 (link).
NMR experiments were performed using a 700 MHz Varian NMR spectrometer or 800 MHz Bruker spectrometer equipped with a cryoprobe. All NMR samples contained 0.5–1.0 mM 2H/15N-EmrE in buffer conditions of 2 mM TPP+, 20 mM NaCl, 20 mM potassium phosphate, 2 mM TCEP, pH 7.0, 45°C. The membrane mimetic in each sample (DDM micelles or isotropic bicelles) is as listed. The TROSY-selected ZZ-exchange experiment35 (link) was modified to include a lipid “flipback” pulse. Data were processed and analyzed with NMRPipe46 (link), NMRView47 (link), Sparky48 , and IgorPro (Wavemetrics). All EmrE structure figures were created in PyMOL using PDB 3B5D with the backbone rebuilt to render the cartoons. Full page versions of the spectra in the main figures are included in the supplementary information.
Publication 2011
1,2-hexanoylphosphatidylcholine Amino Acids Buffers Detergents Dietary Fiber dilauroyl lecithin Dimyristoylphosphatidylcholine dodecyl maltoside Extinction, Psychological Fluorescence Resonance Energy Transfer Freezing Lipids Liposomes Micelles Microscopy, Fluorescence potassium phosphate Proteins Pulse Rate Reflex Sodium Chloride Thrombin Tissue, Membrane Tissue Donors tris(2-carboxyethyl)phosphine Vertebral Column

Most recents protocols related to «Dimyristoylphosphatidylcholine»

Protein kinase A, lactate dehydrogenase, and phosphoenol-pyruvate were purchased from Roche CustomBiotech (Indianapolis, IN). Adenosine-5′-triphosphate disodium salt (ATP) ultrapure 98% was obtained from Alfa Aesar (Tewksbury, MA). Verapamil was acquired from Sigma Aldrich (Saint Louis, MO). n-dodecyl-β-D-maltopyranoside (DDM) was bought from Inalco S. p.A (Milano, Italy). Nicotinamide adenine dinucleotide (NADH) was purchased from Sigma-Aldrich (Burlington, MA).
E. coli polar lipids (polar extract) and synthetic lipids were acquired from Avanti (Alabaster, AL); these include 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine or 16:0-18:1 PC (POPC), 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylethanolamine (POPE), 1-palmitoyl-2-oleoyl-sn-glycero-3-phospho-L-serine (POPS), 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylinositol (POPI), 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphatidylglycerol (POPG), DPPA, 1,2-dipalmitoyl-sn-glycero-3-phosphate or 16:0 PA, 1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC). Sphingomyelin (SM) was >99% pure from porcine brain with major acyl chains of 18:0 (50%) and 21:1 (21%), and cardiolipin (CL) was from >99% bovine heart with major acyl chains of 18:2 (90%). All synthetic lipids, SM and CL had very low tryptophan fluorescence (ex/em 295/350 nm) if purchased as powder. Cholesterol (Chol) and cholesteryl hemisuccinate (CHS) were purchased from Anatrace (Maumee, OH).
General chemicals were at the highest grade from Thermo Fisher Scientific (Waltham, Massachusetts).
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Publication 2023
1-palmitoyl-2-oleoylphosphatidylcholine Adenosine Triphosphate Alabaster Brain Cardiolipins Cattle Cholesterol cholesterol-hemisuccinate Coenzyme I Cyclic AMP-Dependent Protein Kinases Dimyristoylphosphatidylcholine Escherichia coli Fluorescence Glycerylphosphorylcholine Heart Lactate Dehydrogenase Lipids Phosphates Phosphatidylethanolamines Phosphatidylglycerols Phosphatidylinositols Phosphoenolpyruvate Pigs Powder Serine Sodium Chloride Sphingomyelins Tryptophan Verapamil
One million HEK293T cells
were seeded in 6 well plates and grown for 48 h at 37 °C and
5% CO2 atmosphere in high-glucose (c =
4.5 g/L) DMEM with FBS. The cells were washed three times with ice-cold
PBS solution (pH 7.4). For extraction of extracellular metabolites,
50 μL of the medium was transferred into a reaction vial (Eppendorf
low binding tube, 1.5 mL, Eppendorf, Hamburg, Germany) containing
450 μL ice-cold MeOH:H2O (8:1, v/v). The samples
were vortexed for 20 s and centrifuged for 5 min at 16,100g and 4 °C. 200 μL of the supernatant were transferred
into a reaction vial (Eppendorf low binding tube, 1.5 mL, Eppendorf,
Hamburg, Germany) and dried using a rotary vacuum evaporator (Eppendorf
Concentrator Plus, Eppendorf, Hamburg, Germany). The dried samples
were stored at −80 °C for further LC-MS analysis. For
simultaneous proteo-metabolome liquid–liquid extraction (SPM-LLE),
500 μL ice-cold methanol (MeOH) were added to the cells together
with 20 μL of the [U-13C]-labeled yeast extract and
1 μL of the lipid standard (1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC, c = 0.2 mM), 1,2-dimyristoyl-sn-glycero-3-phosphorylethanolamine (DMPE, c = 0.2 mM), 1,2,3-trimyristoyl-glycerol (TMG, c =
0.2 mM)), followed by 500 μL ice-cold water. Efficient cell
lysis was ensured by shear forces generated by pipetting the methanol–water
solution up and down 20 times using a P1000 pipet. Lysates were transferred
into a reaction tube (Eppendorf low binding tube, 2 mL, Eppendorf,
Hamburg, Germany), followed by addition of 500 μL ice-cold chloroform
(CHCl3) and incubation for 20 min at 4 °C and 500
rpm on a thermo-shaker. Afterward, samples were centrifuged for 5
min at 4 °C and 16,000g. The polar and the nonpolar
phase were transferred into two new and separate reaction vials (Eppendorf
low binding tube, 1.5 mL, Eppendorf, Hamburg, Germany), evaporated
to dryness using an Eppendorf Concentrator Plus (Eppendorf, Hamburg,
Germany), and stored at −80 °C for further LC-MS analysis.
The solid interphase pellet was evaporated to dryness using an Eppendorf
Concentrator Plus (Eppendorf, Hamburg, Germany) and stored at −80
°C for proteome extraction.
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Publication 2023
1,2-dimyristoylphosphatidylethanolamine Atmosphere Cells Chloroform Cold Temperature Dimyristoylphosphatidylcholine Glucose Glycerin Glycerylphosphorylcholine Interphase Lipids Liquid-Liquid Extraction Metabolome Methanol phosphoethanolamine Proteome Vacuum Yeast, Dried
HPLC-grade acetonitrile (ACN), methanol (MeOH),
formic acid (FA), as well as Micro BCA Protein Assay Kit, Gibco Qualified
FBS, and ammonium bicarbonate were obtained from Thermo Fisher Scientific
(Dreieich, Germany). Dithiothreitol, iodoacetamide, HPLC-grade chloroform
(CHCl3), urea, sodium deoxycholate (SDC), triethylammonium
bicarbonate (TEAB), ethylenediaminetetraacetic acid (EDTA), Sera-Mag
magnetic carboxylate modified hydrophilic and hydrophobic beads were
obtained from Merck and Sigma-Aldrich (Munich, Germany). Dulbecco’s
Modified Eagle Medium (DMEM), sodium dodecyl sulfate (SDS), sequencing
grade modified trypsin, and HLB 1 cm3 (30 mg) extraction
cartridges, were purchased from PAN Biotech (Aidenbach, Germany),
Carl Roth (Karlsruhe, Germany), Promega (Walldorf, Germany), and Waters
Oasis (Vienna, Austria), respectively. [U-13C]-labeled
yeast extract was purchased from ISOtopic Solutions (Vienna, Austria).
1,2-Dimyristoyl-sn-glycero-3-phosphocholine (DMPC)
and 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine
(DMPE) were obtained from Avanti Polar Lipids (Alabaster, AL, USA),
and 1,2,3-trimyristoyl-glycerol (TMG) was purchased from EDQM (Strasbourg,
France).
[U-13C]-labeled yeast extract of Pichia pastoris (2 billion cells, ISOtopic solutions, Vienna,
Austria) was reconstituted in 2 mL HPLC–H2O aliquoted
and stored at −80 °C. 1,2- Dimyristoyl-sn-glycero-3-phosphocholine (DMPC, dissolved in CHCl3, Avanti
Polar Lipids, Alabaster, AL, USA), 1,2-dimyristoyl-sn-glycero-3-phosphoethanolamine (DMPE, dissolved in CHCl3:MeOH 65:35, v/v; Avanti Polar Lipids, Alabaster, AL, USA), and 1,2,3-trimyristoyl-glycerol
(TMG, dissolved in CHCl3, EDQM, Strasbourg, France) were
combined and evaporated to dryness. The lipid film was taken up in
a mixture of CHCl3:MeOH:H2O (65:35:8, v/v/v)
leading to the final concentration of 0.2 mM for each standard. The
lipid standard was aliquoted and stored under argon at −80
°C. All experiments were performed using five independent experiments
(biological replicates).
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Publication 2023
1,2-dimyristoylphosphatidylethanolamine acetonitrile Alabaster ammonium bicarbonate Argon Biological Assay Biopharmaceuticals Cells Chloroform Deoxycholic Acid, Monosodium Salt Dimyristoylphosphatidylcholine Dithiothreitol Eagle Edetic Acid formic acid Glycerin Glycerylphosphorylcholine High-Performance Liquid Chromatographies Iodoacetamide Isotopes Komagataella pastoris Lipids Methanol Phosphatidylethanolamines Promega Proteins Serum Sulfate, Sodium Dodecyl Trypsin Urea Yeast, Dried
RPMI‐1640 medium was purchased from HyClone (Logan, USA). Fetal bovine serum (FBS), 2‐mercaptoethanol (2‐ME), L‐glutamine, nonessential amino acids, sodium pyruvate, penicillin, and streptomycin were purchased from Invitrogen Gibco (BRL, USA). 4‐(2‐Hydroxyethyl)‐1‐piperazineethanesulfonic acid (HEPES), cholesteryl oleate, OXA, DNFB, and DNBS were purchased from Sigma‐Aldrich Co. (St. Louis, MO). 1,2‐Dimyristoyl‐sn‐glycero‐3‐phosphocholine (DMPC) was obtained from Avanti Polar Lipids Inc. (Alabaster, AL). α‐Peptide (DWFKAFYDKVAEKFKEAF‐NH2) and α‐melittin (DWFKAFYDKVAEKFKEAF‐GSG‐GIGAVLKVLTTGLPALISW‐IKRKRQQ‐NH2) peptides were synthesized by Apeptide Co., Ltd. (Shanghai, China). Melittin was purchased from Bankpeptide Co., Ltd. (Hefei, China). DEX was purchased from Tianya Jin Kinyork Group Co., Ltd. (Hubei, China).
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Publication 2023
2,4-dinitrofluorobenzene sulfonic acid 2-Mercaptoethanol Acids Alabaster Amino Acids cholesteryl oleate Dimyristoylphosphatidylcholine Dinitrofluorobenzene Fetal Bovine Serum Glutamine Glycerylphosphorylcholine HEPES Lipids Melitten Penicillins Peptides Pyruvate Sodium Streptomycin
Recombinant WT and Q252X human apoA-V were obtained from DNA-protein Technologies LLC in Oklahoma City (www.DNA-Protein.com)31 (link),32 (link) or the laboratory of W. Sean Davidson at the University of Cincinnati33 (link). Proteins were solubilized according to the method described by Castleberry et al.33 (link) into a final buffer of 10mM NH4HCO3 with 5mM DTT, pH7.8. Protein concentration was determined using Pierce Microplate BCA Protein Assay Kit – Reducing Agent Compatible (Thermo Fisher, Waltham, MA).
For HX MS, apoA-V protein was freshly dialyzed from 6M GdnHCl with 10mM DTT into 50mM sodium citrate buffer (pH 3.8) at 4°C before use. Protein concentration was determined by absorbance at 280 nm. Small unilamellar vesicles (SUV, ~20nm diameter) of dimyristoyl phosphatidylcholine (DMPC) (Avanti Polar Lipids, Alabaster AL) at 10mg/ml in aqueous buffer were prepared by sonication34 (link).
Publication Preprint 2023
Alabaster Apolipoprotein A5 Apolipoproteins A Biological Assay Buffers Dimyristoylphosphatidylcholine Homo sapiens HSP40 Heat-Shock Proteins Lipids Proteins Reducing Agents Sodium Citrate Unilamellar Vesicles

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1,2-dimyristoyl-sn-glycero-3-phosphocholine is a synthetic phospholipid commonly used in research applications. It is a common component of cell membranes and can be used to model lipid bilayers.
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1,2-dimyristoyl-sn-glycero-3-phosphocholine (DMPC) is a synthetic phospholipid compound. It is commonly used as a model membrane system in various biophysical and biochemical studies.
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Cholesterol is a lab equipment product that measures the concentration of cholesterol in a given sample. It provides quantitative analysis of total cholesterol, HDL cholesterol, and LDL cholesterol levels.
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1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine is a phospholipid consisting of a glycerol backbone with a palmitic acid and an oleic acid esterified to the first and second carbons, respectively, and a phosphocholine group attached to the third carbon. This compound is a commonly used lipid in various biochemical and biophysical applications.
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Chloroform is a colorless, volatile liquid with a characteristic sweet odor. It is a commonly used solvent in a variety of laboratory applications, including extraction, purification, and sample preparation processes. Chloroform has a high density and is immiscible with water, making it a useful solvent for a range of organic compounds.
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1,2-dipalmitoyl-sn-glycero-3-phosphocholine is a synthetic phospholipid commonly used as a model system for the study of lipid membranes and their properties. It has a molecular formula of C40H80NO8P and is composed of two palmitoyl fatty acid chains attached to a glycerol backbone, with a phosphocholine head group.
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NaCl is a chemical compound commonly known as sodium chloride. It is a white, crystalline solid that is widely used in various industries, including pharmaceutical and laboratory settings. NaCl's core function is to serve as a basic, inorganic salt that can be used for a variety of applications in the lab environment.
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1,2-dioleoyl-sn-glycero-3-phosphocholine is a synthetic lipid compound. It is a phospholipid that consists of two oleic acid chains attached to a glycerol backbone, with a phosphocholine headgroup.
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1,2-dimyristoyl-sn-glycero-3-phospho-(1′-rac-glycerol) is a phospholipid compound. It is a synthetic dialkyl glycerophospholipid.
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Bio-Beads SM-2 are macroporous polystyrene beads designed for size exclusion chromatography. They have a porous structure that allows for the separation of molecules based on their size and shape. The beads have a specified surface area and pore size distribution.

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