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Trifluoroethanol

Q: How can Trifluoroethanol be used in protein research?

Trifluoroethanol's high polarity and hydrogen bonding ability make it useful for studying protein structure and folding. Researchers can use Trifluoroethanol to induce or stabilize specific protein conformations, which can provide insights into the fundamental mechanisms of protein folding and dynamics.

Trifluoroethanol is a fluorinated alcohol compound with the chemical formula C2H3F3O.
It is a clear, colorless liquid with a characteristic odor.
Trifluoroethanol is widely used as a solvent in organic synthesis and as a reagent in biochemical and pharmaceutical research.
It exhibits unique properties, such as high polarity, hydrogen bonding ability, and a high dielectric constant, making it a valuable tool for studying protein structure and folding.
Trifluoroethnal is also known for its potential applications in the development of new materials and the synthesis of fluorinated compounds.
Researchers can leverage the power of PubCompare.ai to discover the best protocols and methods for their Trifluoroethanl experiments, enhancing reproducibility and optimizing their research workflows.

Most cited protocols related to «Trifluoroethanol»

Drosophila Embryo Lysis and Shearing

In all experiments involving the use of yeast, lysis was performed using a mechanical bead
beating procedure in 1% SDS-containing buffer. In all HeLa, mESC, and NP experiments, lysis
was performed using 1% SDS-containing buffer with Benzonase treatment to shear chromatin.
Details of yeast, HeLa, mESC, and NP lysis, reduction, and alkylation protocols are given in the
Supplementary Information.
Drosophila embryos were lysed using a solution-based procedure with sonication.
Single embryos in PCR tubes were re-suspended in 20 μl of lysis buffer containing
20 μg of SP3 beads. Lysis buffer was composed of 1% SDS (Bio-Rad), 1×
cOmplete Protease Inhibitor Cocktail-EDTA (Roche), 5 mM EDTA, 5 mM EGTA, 10 mM
NaOH, and 10 mM DTT, in 10 mM HEPES buffer at pH 8.5 (Sigma). The lysis solution was
combined with 20 μl of neat trifluoroethanol (Sigma) and sonicated for 15 min
in a Bioruptor (Diagenode) for 10 cycles (30 s on, 30 s off) on the setting
‘high’. The Bioruptor was operated in the absence of active cooling to allow the water
bath to heat and facilitate lysis and shearing of chromatin. To neutralize the lysis solution,
0.75 μl of 0.1% formic acid was added. Samples were then heated at 95°C
for 5 min and placed on ice before proceeding with reduction and alkylation steps. (Details
of reduction and alkylation can be found in the Supplementary Information.)

Hughes C.S., Foehr S., Garfield D.A., Furlong E.E., Steinmetz L.M, & Krijgsveld J. (2014). Ultrasensitive proteome analysis using paramagnetic bead technology. Molecular Systems Biology, 10(10), 1-10.

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Publication 2014

Alkylation Benzonase Buffers Chromatin Drosophila Edetic Acid Egtazic Acid Embryo formic acid HeLa Cells HEPES Mouse Embryonic Stem Cells Protease Inhibitors Trifluoroethanol Yeast, Dried

Proteomic Workflow for HeLa and E. coli

Human cervical cancer cells (HeLa S3, ATCC, Manassas, VA) were grown in Dulbecco's modified Eagle's medium with 10% fetal bovine serum, 20 mm glutamine and 1% penicillin-streptomycin (all Life Technologies Ltd., Paisley, UK). Escherichia coli (strain: XL1 blue) was cultured at 37 °C in LB medium until logarithmic phase (optical density = 0.5, λ = 600 nm). Cells were collected by centrifugation. Following a washing step with cold phosphate buffered saline, they were pelleted and flash frozen in liquid nitrogen and stored at −80 °C.
One-device cell lysis, reduction, and alkylation was performed in sodium deoxycholate (SDC) buffer with chloroacetamide (PreOmics GmbH, Martinsried, Germany) according to our previously published protocol (32 (link)). Briefly, the cell suspension was twice boiled for 10 min at 95 °C and subsequently sonicated for 15 min at maximum energy (Bioruptor, Diagenode, Seraing, Belgium). Proteins were enzymatically hydrolyzed overnight at 37 °C by LysC and trypsin (1:100 enzyme:protein (wt/wt) for both). To stop the digestion, the reaction mixture was acidified with five volumes of isopropanol with 1% trifluoroacetic acid (TFA). Peptides were de-salted and purified in two steps, first on styrenedivinylbenzene-reversed phase sulfonate (SDB-RPS), and second on C₁₈ sorbent. The dried eluates were re-constituted in water with 2% acetonitrile (ACN) and 0.1% TFA for direct LC-MS analysis or high pH reversed-phase fractionation.
For the experiments with the Evosep One (see below), HeLa cell pellets were re-suspended and lysed in water/trifluoroethanol. Disulfide bonds were reduced with dithiothreitol and alkylated with iodoacetamide in ammonium bicarbonate buffer. Following tryptic digestion, the peptide mixture was de-salted and purified on C₁₈ sorbent.

Meier F., Brunner A.D., Koch S., Koch H., Lubeck M., Krause M., Goedecke N., Decker J., Kosinski T., Park M.A., Bache N., Hoerning O., Cox J., Räther O, & Mann M. (2018). Online Parallel Accumulation–Serial Fragmentation (PASEF) with a Novel Trapped Ion Mobility Mass Spectrometer. Molecular & Cellular Proteomics : MCP, 17(12), 2534-2545.

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Publication 2018

acetonitrile Alkanesulfonates Alkylation ammonium bicarbonate Buffers Cells Centrifugation Cervical Cancer chloroacetamide Cold Temperature Culture Media Deoxycholic Acid, Monosodium Salt Digestion Disulfides Dithiothreitol Enzymes Escherichia coli Fetal Bovine Serum Fractionation, Chemical Freezing Glutamine HeLa Cells Homo sapiens Iodoacetamide Isopropyl Alcohol Medical Devices Nitrogen Pellets, Drug Penicillins Peptides Phosphates Proteins Saline Solution Strains Streptomycin Trifluoroacetic Acid Trifluoroethanol Trypsin

Structural Insights into RIG-I Helicase-RD Binding to dsRNA

Recombinant full-length RIG-I (1–925), helicase-RD (232–925), helicase (232–794), RD (795–925), and selenomethione derivatized helicase-RD were expressed in Escherichia coli and purified to homogeneity using immobilized metal ion affinity, hydroxyapatite and heparin affinity chromatography. Fluorescence anisotropy titrations were performed at 25°C^{30 (link)} (λ_excitation 494 nm and λ_emission 516 nm) using a fluorescein-labeled 14 base pair dsRNA prepared by annealing 5′GGAGAGAACCGCCU and 3′CCUCUCUUGGCGGA-F RNA, where F is fluorescein. Crystals of the native and selenomethione helicase-RD with pal-dsRNA (5′CGACGCUAGCGUCG) and ADP•BeF₃•Mg²⁺ were obtained in 25% (w/v) PEG 3350, 0.25 M NaSCN, 100 mM MOPS (pH 7.8), 3% (v/v) 2,2,2-Trifluoroethanol at 20°C by hanging drop. The crystals belong to space group P6₅22 with cell parameters a=b=174.9 Å and c=110.9 Å. The structure was determined by SAD to 3.2 Å resolution and refined against a 2.9 Å resolution native data set. The final model has an R_work and R_free of 0.199 and 0.287, respectively. SAXS measurements were preformed on full-length RIG-I and helicase-RD in the absence and presence of dsRNA (5′GCGCGCGCGC). Buffer subtraction and R_g were calculated from Guinier plots. D_max was determined by scanning a range of values and comparing experimental I(s) values to P(r) transforms. Ten ab initio models were averaged and normalized spatial discrepancy (NSD) values were calculated. The helicase-RD•dsRNA and a homologous CARD structure were positioned into the ab initio model and χ² were determined.

Jiang F., Ramanathan A., Miller M.T., Tang G.Q., Gale M J.r., Patel S.S, & Marcotrigiano J. (2011). Structural Basis of RNA Recognition and Activation by Innate Immune Receptor RIG-I. Nature, 479(7373), 423-427.

Publication 2011

Anisotropy, Fluorescence Base Pairing Buffers Cells Chromatography, Affinity DDX58 protein, human DNA Helicases Durapatite Escherichia coli Fluorescein Heparin Metals morpholinopropane sulfonic acid polyethylene glycol 3350 RNA, Double-Stranded sodium thiocyanate Titrimetry Trifluoroethanol

Synthesis and Purification of Surfactant Peptides

MB (34 amino acid sequence: NH2-CWLCRALIKRIQAMIPKGGRMLPQLVCRLVLRCSCOOH; see Fig. 2B), S-MB (41 amino acid sequence: NH2-FPIPLPYCWLCRALIKRIQAMIPKGGRMLPQLVCRLVLRCS-COOH; see Fig. 2A) and SP-B(1–8) [8 amino acid sequence: NH2-FPIPLPYC-CONH2] were prepared with either a ABI 431A solid phase peptide synthesizer (Applied Biosystems, Foster City, CA) configured for FastMoc™ chemistry [54] (link), a Symphony Multiple Peptide Synthesizer (Protein Technologies, Tucson, AZ) using standard Fmoc synthesis, or a Liberty Microwave Peptide Synthesizer (CEM Corp., Matthews, NC) configured for standard Fmoc synthesis. A low substitution (0.3 mmole/gm) pre-derivatized Fmoc-serine (tBu) Wang resin (NovaBiochem, San Diego, CA) or H-Ser(OtBu)-HMPB Nova PEG resin (NovaBiochem, San Diego, CA) were used to minimize the formation of truncated sequences with the MB and S-MB peptide, while a Rink Amide MBHA resin (NovaBiochem, San Diego, CA) was employed for synthesis of the SP-B(1–8) peptide. All residues were double-coupled to insure optimal yield [48] (link). After synthesis of the respective linear sequences, peptides were cleaved from the resin and deprotected using a mixture of 0.75 gm phenol, 0.25 ml ethanedithiol, 0.5 ml of thioanisole, 0.5 ml of deionized water and 10 ml trifluoroacetic acid per gram of resin initially chilled to 5°C, and then allowed to come to 25°C with continuous stirring over a period of 2 h to insure complete peptide deprotection [48] (link). Crude peptides were removed from the resin by vacuum-assisted filtration, and by washing on a medium porosity sintered glass filter with trifluoroacetic acid and dichloromethane to maximize yield. Filtered crude peptides were precipitated in ice cold tertiary butyl ether, and separated by centrifugation at 2000×g for 10 min (2–3 cycles of ether-precipitation and centrifugation were used to minimize cleavage-deprotection byproducts). Reduced crude peptides from ether-precipitation were verified for molecular mass by MALDI-TOF spectroscopy, dissolved in trifluoroethanol (TFE):10 mM HCl (1∶1, v∶v), freeze dried, and purified by preparative HPLC [48] (link). Final folding of HPLC-purified peptides was facilitated by air-oxidation for at least 48 h at 25°C in TFE and 10 mM ammonium bicarbonate buffer (4∶6, v∶v) at pH 8.0 [55] (link). Final oxidized MB and S-MB were re-purified by reverse phase HPLC, verified in molecular mass via MALDI-TOF, and disulfide connectivity was confirmed by mass spectroscopy of enzyme-digested fragments (trypsin and chymotrypsin digestion).

Walther F.J., Waring A.J., Hernandez-Juviel J.M., Gordon L.M., Wang Z., Jung C.L., Ruchala P., Clark A.P., Smith W.M., Sharma S, & Notter R.H. (2010). Critical Structural and Functional Roles for the N-Terminal Insertion Sequence in Surfactant Protein B Analogs. PLoS ONE, 5(1), e8672.

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Publication 2010

Amino Acid Sequence ammonium bicarbonate Anabolism Buffers Centrifugation Chymotrypsin Cold Temperature Cytokinesis Digestion Disulfides Enzymes ethanedithiol Ethers Ethers, Cyclic Filtration Freezing High-Performance Liquid Chromatographies Mass Spectrometry Methylene Chloride methylphenylsulfide Microwaves Peptides Phenol Proteins Resins, Plant Rink amide resin Serine Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Spectrum Analysis Trifluoroacetic Acid Trifluoroethanol Trypsin Vacuum Wang resin

Synthesis and Characterization of PEGylated Conjugates

N-α-Fmoc protected amino acids, 2-(1H-benzotriazol-1-yl)-1,1,3,3-tetramethyluronium hexafluorophosphate (HBTU) and 2-Cl-trityl chloride resin (100–200 mesh, 1.27 mmol/g) were from EMD Biosciences (San Diego, CA). Papain (EC 3.4.22.2, from papaya latex) and cathepsin B (EC 3.4.22.1, from bovine spleen) were from Sigma-Aldrich (St. Louis, MO). Bis-MAL-dPEG3 (bis-[1,13-(3-maleimidopropionyl)amido]-4,7,10-trioxatridecane, CAS# 756525-89-0) was purchased from Quanta Biodesign (Powell, OH). 1-Hydroxybenzotriazole (HOBt) was purchased from AnaSpec (Fremont, CA). N,N′-Diisopropylcarbodiimide (DIC), 2,2,2-trifluoroethanol (TFE) and all other reagents and solvents were from Sigma-Aldrich (St. Louis, MO). Doxorubicin (DOX) was a kind gift from Meiji Seika Kaisha Ltd. Tokyo, Japan. HPMA,14 4-cyanopentanoic acid dithiobenzoate15 were synthesized according to literature. N-Methacryloylglycylphenylalanylleucylglycyl-doxorubicin (MA-GFLG-DOX) was prepared by the reaction N-methacryloylglycylphenylalanylleucylglycine 4-nitrophenyl ester (MA-GFLG-ONp) with doxorubicin hydrochloride in DMF in the presence of diisopropylethylamine according to the described procedure.16
UV-vis spectra were measured on a Varian Cary 400 Bio UV-visible spectrophotometer. Mass spectra were measured on an FTMS mass spectrometer (LTQ-FT, ThermoElectron, Waltham, MA). ¹H-NMR spectra were recorded on a Mercury400 spectrometer using DMSO-d₆ as the solvent. Polymerization conversion was determined by the measurement of remaining HPMA monomer concentration at different time points using RP-HPLC (Agilent Technologies 1100 series, Zorbax C8 column 4.6×150 mm) with gradient elution from 2 to 90% of Buffer B within 30 min at flow rate of 1.0 mL/min (Buffer A: deionized water (DI H₂O) with 0.1% TFA, Buffer B: acetonitrile with 0.1% TFA). The molecular weight and polydispersity index (PDI) of polymers were measured on an ÄKTA FPLC (fast protein liquid chromatography) system (GE Healthcare, formerly Amersham) equipped with miniDAWN TREOS and OptilabEX detectors (Wyatt Technology, Santa Barbara, CA) using a Superose 6 or 12 HR10/30 column with PBS (pH 7.3) as the mobile phase. Narrow polydispersity polyHPMA fractions prepared by size exclusion chromatography, whose molecular weights were characterized by multiangle light scattering, were used as molecular weight standards. The multiblock polymers were fractionated on the same FPLC system using Superose 6 HR16/60 preparative column. PBS was used as the mobile phase. The flow rate was 1 mL/min. the fraction was collected every 10 min. The salt in the fractions was removed by dialysis. The narrow polydispersity polymer fractions were obtained after freeze-drying.

Pan H., Yang J., Kopečková P, & Kopeček J. (2010). Backbone Degradable Multiblock N-(2-Hydroxypropyl)methacrylamide Copolymer Conjugates via Reversible Addition Fragmentation Chain Transfer Polymerization and Thiol-ene Coupling Reaction. Biomacromolecules, 12(1), 247-252.

Publication 2010

1-hydroxybenzotriazole 1H NMR acetonitrile Acids Amino Acids Bos taurus Buffers Carica papaya Cathepsin B Dialysis Doxorubicin Duxon Esters Gel Chromatography High-Performance Liquid Chromatographies Hydrochloride, Doxorubicin hydroxypropyl methacrylate Latex Light Liquid Chromatography Mass Spectrometry Papain Polymerization Polymers Proteins Resins, Plant Sodium Chloride Solvents Spleen Sulfoxide, Dimethyl Trifluoroethanol trityl chloride

Most recents protocols related to «Trifluoroethanol»

Electrospun Nanofiber Composites for Applications

Gelatin powder from bovine skin (GEL, type B), polycaprolactone (PCL, M_n ~ 80,000), poly (vinylidene fluoride) (PVDF, M_w ~ 275,000), polystyrene (PS, M_w ~ 280,000), nylon 6/6 (NY) were selected as the solute of electrospinning solution and denoted as NY, PCL/GEL, PVDF, and PS, respectively. N, n-dimethylformamide (DMF, ≥ 99.9%), 2,2,2-trifluoroethanol (TFE, ≥ 99.0%), formic acid (≥ 98.0%), chloroform (≥ 99.5%), methanol (≥ 99.5%), and acetone (≥ 99.7%) were utilized for the solvent of electrospinning solution. All solutes and solvents were provided from Sigma–Aldrich (USA). Tetrabutylammonium bromide (TBAB, ≥ 99.0%) was also obtained from Sigma–Aldrich (USA). Potassium chloride (KCl, ≥ 99.0%) and deionized (DI) water were acquired from Duksan Chemical Co., Ltd. (South Korea). Sylgard® 184 polydimethylsiloxane (PDMS) silicone elastomer base monomer and hardener were bought from Dow Corning (USA). All ingredients and materials were utilized without further purification.

Song J.Y., Kim S., Park J, & Park S.M. (2023). Highly Efficient, Dual-Functional Self-Assembled Electrospun Nanofiber Filters for Simultaneous PM Removal and On-Site Eye-Readable Formaldehyde Sensing. Advanced Fiber Materials, 5(3), 1088-1103.

Publication 2023

Acetone Bos taurus Chloroform Dimethylformamide formic acid Gelatins Methanol nylon 6 polycaprolactone polydimethylsiloxane Polystyrenes polyvinylidene fluoride Powder Silicone Elastomers Skin Solvents tetrabutylammonium bromide Trifluoroethanol

NMR Analysis of Synthetic Peptides

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Publication 2023

Nuclear Magnetic Resonance, Heteronuclear Peptides Trifluoroethanol

Conformational Changes of A11 Peptide

To observe the conformational change of A11 induced by membrane-mimicking environmental conditions, the secondary structure of A11 peptide was investigated by CD analysis using a Jasco-815 spectropolarimeter (Jasco, Japan). Peptide solutions were diluted to a final concentration of 150 µM in different environments: deionized water (aqueous environment), 30 mM sodium dodecyl sulfate (SDS; mimicking the negative charge of prokaryotic membranes), and 50% (vol/vol) TFE (2,2,2-trifluoroethanol; mimicking the hydrophobicity of bacterial membranes). CD spectra were recorded at 10 nm/min scanning speed in the spectral range of 190 to 250 nm, with a 0.1-mm-path length quartz cell at room temperature. Three scans were performed for each environment. The acquired CD spectrum was converted to the mean residue ellipticity using the following equation:

θ_{M} = (θ_{obs} / 10) \times (M_{RW} / c \times 1)

where θ_M is residue ellipticity (deg./M/m), θ_obs is observed ellipticity corrected for the buffer at a given wavelength (mdeg), M_RW is residue molecular weight (M_W/number of amino acids), c is concentration of peptide (mg/ml), and 1 is the path length (cm).

Sengkhui S., Klubthawee N, & Aunpad R. (2023). A novel designed membrane-active peptide for the control of foodborne Salmonella enterica serovar Typhimurium. Scientific Reports, 13, 3507.

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Publication 2023

Amino Acids Bacteria Buffers Cells Peptides Prokaryotic Cells Quartz Radionuclide Imaging Sulfate, Sodium Dodecyl Tissue, Membrane Trifluoroethanol

Electrochemical Oxidation of Organic Substrates

The as-prepared NiHC-pz-300 catalyst (12.5 mg) was dispersed in 968 μL absolute ethanol and 32 μL Nafion solution (5 wt%) accompanied by a continuous ultra-sonification to form a homogeneous catalyst ink. Then, 40 μL ink was pipetted onto the double sides of carbon paper, giving a catalyst loading of 1 mg cm⁻². The catalyst with lower loadings was prepared by diluting the ink with ethanol. The electrochemical workstation (CHI 660E, Shanghai CH Instruments Co., China) was utilized for the electrochemical studies. The electrochemical measurements were carried out in a typical H-Type cell with three-electrode configuration, which consists of the as-prepared NiHC-pz-300 catalyst electrode as the working electrode, a platinum foil as the auxiliary electrode, and a Ag/AgCl (saturated KCl) as the reference electrode. All measured potentials were converted to the reversible hydrogen electrode (RHE) according to the following equation:

E (RHE) = E (Ag / AgCl) + 0.197 + 0.0591 \times pH

The electrochemical oxidation activity of 25 organic substrates (methanol, ethanol, 2,2,2-trifluoroethanol, benzyl alcohol, 2-propanol, 1,1,1-trifluoro-2-propanol, 1-phenylethanol, benzaldehyde, furfural, ethylene glycol, 1,4-butanediol, 1,6-hexanediol, ethylamine, 1-propylamine, 2,2,2-trifluoroethylamine, benzylamine, 2-propylamine, 1-phenylethylamine, cyclohexanol, cyclohexylamine, urea, glycerol, glucose, 5-hydroxymethylfurfural and 2-aminoethanol) were evaluated in 1 M KOH + 0.1 M substrate. The Linear sweep voltammetry (LSV) curves were scanned at a rate of 5 mV s⁻¹ at room temperature after 5 cyclic voltammetry (CV) cycles at a scan rate of 50 mV s⁻¹. All polarization curves were manually corrected with 90% iR-compensation. For obtaining accurate Tafel slope values, all Tafel plots were iR-corrected. Chronopotentiometric measurements were recorded at a current density of 20 mA cm⁻². In order to reduce the impact on the stability of the catalyst due to the changes of substrate concentration, the electrolyte was refreshed every 12 h. Turnover frequencies (TOFs) were calculated from the following equation:

TOF = \frac{I}{n F c}

where I is the current density in the LSV curve (mA/mg), n is the number electrons needed for the oxidation of one urea molecule (n = 6 (N₂) or 12 (NO₂⁻)), F is the Faraday constant of 96485 F/mol, c is the active Ni site density in the catalyst (mol/g).

Chen Z., Li J., Meng L., Li J., Hao Y., Jiang T., Yang X., Li Y., Liu Z.P, & Gong M. (2023). Ligand vacancy channels in pillared inorganic-organic hybrids for electrocatalytic organic oxidation with enzyme-like activities. Nature Communications, 14, 1184.

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Publication 2023

1-phenylethanol 1-Propanol 2-propylamine 5-hydroxymethylfurfural benzaldehyde Benzyl Alcohol Benzylamines Butylene Glycols Carbon Cells Cyclohexanol Cyclohexylamines Electrolytes Electrons Ethanol Ethanolamine ethylamine Furaldehyde Glucose Glycerin Glycol, Ethylene Hydrogen Isopropyl Alcohol Methanol Nafion Phenethylamines Platinum Propylamines Radionuclide Imaging Trifluoroethanol trifluoroethylamine Urea

Electrochemical Synthesis of Ni-based MOFs

All reagents were used as received without further purification. Nickel chloride hexahydrate (NiCl₂·6H₂O), pyrazine, pyrimidine, 4,4-bipyridine, ethanol (≥ 99.7%), N,N-dimethylformamide, methanol, 2,2,2-trifluoroethanol, 2-phenylethanol, 1-propanol, 3-propanol, furfural, 1,4-butanediol, 1,6-hexanediol, ethylamine, 1-phenylethylamine, cyclohexanol, cyclohexylamine, 1-propylamine, 2-aminoethanol, urea, glycerol, glucose, 5-hydroxymethylfurfural (5-HMF), ethylene glycol and 1-hexanethiol were all purchased from Aladdin Industrial Corporation (China). Potassium hydroxide (KOH) was purchased from Sinopharm Chemical Reagent Co., Ltd. (China). 1,1,1-trifluoro-2-propanol, 1-phenylethanol, benzaldehyde and 2-propylamine were purchased from Innochem Alfa Acros (China). Methyl mercaptan was purchased from Macklin Biochemical Co., Ltd. (China). 2,2,2-trifluoroethylamine and benzylamine were purchased from Shanghai Titan Scientific Co., Ltd. (China). Ultrapure deionized water (18.2 MΩ·cm⁻¹, 25 ^oC) was obtained from ELGA purification system (China). Anion exchange membrane was obtained from Fumatech (FAB-PK-130, Germany). Carbon fiber paper was purchased from Hesen Electric Co., Ltd. (HCP020N, China).

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Publication 2023

1-phenylethanol 1-Propanol 2-propylamine 5-hydroxymethylfurfural Anions benzaldehyde Benzylamines Butylene Glycols Carbon Fiber Cyclohexanol Cyclohexylamines Dimethylformamide Electricity Ethanol Ethanolamine ethylamine Furaldehyde Glucose Glycerin Glycol, Ethylene Methanol methylmercaptan nickel chloride hexahydrate Phenethylamines Phenylethyl Alcohol PK 130 potassium hydroxide Propylamines Pyrazines Pyrimidines Tissue, Membrane Trifluoroethanol trifluoroethylamine Urea

Top products related to «Trifluoroethanol»

2 2 2 trifluoroethanol by Merck Group

Sourced in United States, United Kingdom, Germany

2,2,2-trifluoroethanol is a colorless, volatile, and high-purity organic compound. It has the chemical formula C2H3F3O. This compound is used as a specialty chemical in various industrial and research applications.

J 810 spectropolarimeter by Jasco

Sourced in Japan, United States, Italy, Germany, United Kingdom, Canada, France

The J-810 spectropolarimeter is a laboratory instrument designed for the measurement of circular dichroism (CD) and other optical rotatory properties of samples. It provides accurate and reliable data on the secondary structure and conformational changes of biological macromolecules such as proteins, nucleic acids, and other chiral compounds.

2 2 2 trifluoroethanol tfe by Merck Group

Sourced in United States, Spain, United Kingdom, France, Germany

2,2,2-trifluoroethanol (TFE) is a fluorinated alcohol compound with the molecular formula C2H3F3O. It is a clear, colorless liquid with a mild odor. TFE is commonly used as a solvent and reagent in various laboratory applications.

Trifluoroethanol by Merck Group

Sourced in United States

Trifluoroethanol is a fluorinated alcohol compound used as a specialty chemical in laboratory settings. It has a high boiling point and is miscible with a variety of organic solvents. Trifluoroethanol serves as a useful solvent and reagent in various chemical synthesis and analysis procedures.

Dithiothreitol (dtt) by Merck Group

Sourced in United States, Germany, United Kingdom, Italy, Sao Tome and Principe, France, China, Switzerland, Macao, Spain, Australia, Canada, Belgium, Sweden, Brazil, Austria, Israel, Japan, New Zealand, Poland, Bulgaria

Dithiothreitol (DTT) is a reducing agent commonly used in biochemical and molecular biology applications. It is a small, water-soluble compound that helps maintain reducing conditions and prevent oxidation of sulfhydryl groups in proteins and other biomolecules.

Polycaprolactone by Merck Group

Sourced in United States, Germany, United Kingdom, Sao Tome and Principe, Poland, India, Italy, China, Belgium, Singapore, Japan, Portugal, Brazil, Spain, Canada, Denmark

Polycaprolactone is a biodegradable polyester material commonly used in laboratory applications. It is a synthetic polymer with a high molecular weight and a low melting point. Polycaprolactone is known for its versatility, biocompatibility, and tailorable physical properties, making it a valuable tool in various scientific and research settings.

J 815 spectropolarimeter by Jasco

Sourced in Japan, United States, Germany, United Kingdom, Italy, Canada

The J-815 spectropolarimeter is a laboratory instrument used for the measurement of circular dichroism (CD) spectra. It is designed to analyze the interaction between polarized light and chiral molecules or structures. The J-815 spectropolarimeter provides accurate and reliable data on the secondary structure and conformational changes of biological macromolecules such as proteins, nucleic acids, and other chiral compounds.

Trypsin by Promega

Sourced in United States, Germany, United Kingdom, China, Japan, France, Switzerland, Sweden, Italy, Netherlands, Spain, Canada, Brazil, Australia, Macao

Trypsin is a serine protease enzyme that is commonly used in cell culture and molecular biology applications. It functions by cleaving peptide bonds at the carboxyl side of arginine and lysine residues, which facilitates the dissociation of adherent cells from cell culture surfaces and the digestion of proteins.

Formic acid by Merck Group

Sourced in Germany, United States, Italy, United Kingdom, France, Spain, China, Poland, India, Switzerland, Sao Tome and Principe, Belgium, Australia, Canada, Ireland, Macao, Hungary, Czechia, Netherlands, Portugal, Brazil, Singapore, Austria, Mexico, Chile, Sweden, Bulgaria, Denmark, Malaysia, Norway, New Zealand, Japan, Romania, Finland, Indonesia

Formic acid is a colorless, pungent-smelling liquid chemical compound. It is the simplest carboxylic acid, with the chemical formula HCOOH. Formic acid is widely used in various industrial and laboratory applications.

J 815 by Jasco

Sourced in Japan, United States, Germany, United Kingdom, Italy

The J-815 is a circular dichroism (CD) spectrometer designed for the analysis of the structural and conformational properties of biological macromolecules. It measures the difference in absorbance of left and right circularly polarized light by a sample, providing information about the secondary structure of proteins, nucleic acids, and other biomolecules.

What are some common uses of Trifluoroethanol?

Trifluoroethanol is widely used as a solvent in organic synthesis and as a reagent in biochemical and pharmaceutical research. Its unique properties, such as high polarity, hydrogen bonding ability, and a high dielectric constant, make it a valuable tool for studying protein structure and folding. Trifluoroethanol is also known for its potential applications in the development of new materials and the synthesis of fluorinated compounds.

How can Trifluoroethanol be used in protein research?

Are there any variations or types of Trifluoroethanol?

While Trifluoroethanol typically refers to the compound with the chemical formula C2H3F3O, there are various fluorinated alcohol compounds that share similar properties and applications. These include compounds like 2,2,2-Trifluoroethanol, which has the same molecular formula but a slightly different structure, and other fluorinated alcohols with varying degrees of fluorination.

What are some potential challenges in using Trifluoroethanol?

One potential challenge with using Trifluoroethanol is its high flammability and toxicity, which requires careful handling and safety precautions. Additionally, Trifluoroethanol can be corrosive to certain materials, so researchers must ensure compatibility with their experimental setup and equipment. Proper solvent disposal and waste management protocols are also important considerations when working with Trifluoroethanol.

How can PubCompare.ai help with Trifluoroethanol research?

PubCompare.ai allows researchers to more efficiently screen protocol liteature related to Trifluoroethanol and leverage AI to pinpoint critical insights. The platform's intelligent comparisons can help you identify the most effective protocols for your specific Trifluoroethanl research goals, enhancing reproducibility and optimizing your workflow. By highlighting key differences in protocol effectiveness, PubCompare.ai can enable you to choose the best option for accuracy and reliability in your Trifluoroethonol experiments.

More about "Trifluoroethanol"

Trifluoroethanol, also known as 2,2,2-trifluoroethanol (TFE), is a fluorinated alcohol compound with the chemical formula C2H3F3O.
It is a clear, colorless liquid with a distinctive odor.
This versatile solvent is widely used in organic synthesis, biochemical research, and pharmaceutical development due to its unique properties.
Trifluoroethanol exhibits a high polarity, strong hydrogen bonding ability, and a high dielectric constant, making it a valuable tool for studying protein structure and folding.
Researchers often employ techniques like circular dichroism (CD) spectroscopy, using instruments like the J-810 or J-815 spectropolarimeters, to analyze the effects of TFE on protein conformation.
In addition to its applications in biochemistry, Trifluoroethanol is also known for its potential in the development of new materials and the synthesis of fluorinated compounds.
It can be used as a reagent in various organic reactions, including those involving dithiothreitol (DTT) and trypsin.
The power of PubCompare.ai can be leveraged to discover the best protocols and methods for Trifluoroethanol experiments, enhancing reproducibility and optimizing research workflows.
This AI-driven platform helps researchers locate the optimal procedures from literature, preprints, and patents, enabling them to refine their Trifluoroethananol-related studies with greater efficiency and confidence.
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