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Amber

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Most cited protocols related to «Amber»

Initial helical conformations were defined as all amino acids having (φ, ψ)=(−60°, −40°). Initial extended conformations were defined as all (φ, ψ)=(180°, 180°). Native conformations, as appropriate, were defined for each system as below. Explicit solvation was achieved with truncated octahedra of TIP3P water16 with a minimum 8.0 Å buffer between solute atoms and box boundary. All structures were built via the LEaP module of Ambertools. Except where otherwise indicated, equilibration was performed with a weak-coupling (Berendsen) thermostat33 and barostat targeted to 1 bar with isotropic position scaling as follows. With 100 kcal mol−1 Å−2 positional restraints on protein heavy atoms, structures were minimized for up to 10000 cycles and then heated at constant volume from 100 K to 300 K over 100 ps, followed by another 100 ps at 300 K. The pressure was equilibrated for 100 ps and then 250 ps with time constants of 100 fs and then 500 fs on coupling of pressure and temperature to 1 bar and 300 K, and 100 kcal mol−1 Å−2 and then 10 kcal mol−1 Å−2 Cartesian positional restraints on protein heavy atoms. The system was again minimized, with 10 kcal mol−1 Å−2 force constant Cartesian restraints on only the protein main chain N, Cα, and C for up to 10000 cycles. Three 100 ps simulations with temperature and pressure time constants of 500 fs were performed, with backbone restraints of 10 kcal mol−1 Å−2, 1 kcal mol−1 Å−2, and then 0.1 kcal mol−1 Å−2. Finally, the system was simulated unrestrained with pressure and temperature time constants of 1 ps for 500 ps with a 2 fs time step, removing center-of-mass translation and rotation every picosecond.
SHAKE34 was performed on all bonds including hydrogen with the AMBER default tolerance of 10−5 Å for NVT and 10−6 Å for NVE. Non-bonded interactions were calculated directly up to 8 Å. Beyond 8 Å, electrostatic interactions were treated with cubic spline switching and the particle-mesh Ewald approximation35 in explicit solvent, with direct sum tolerances of 10−5 for NVT or 10−6 for NVE. A continuum model correction for energy and pressure was applied to long-range van der Waals interactions. The production timesteps were 2 fs for NVT and 1 fs for NVE.
Publication 2015
Amber Amino Acids Buffers Cuboid Bone Debility Electrostatics Helix (Snails) Hydrogen-5 Immune Tolerance nucleoprotein, Measles virus Pressure Proteins Solvents Vertebral Column
MD simulations of hen egg white lysozyme (HEWL), bovine pancreatic trypsin inhibitor (BPTI), ubiquitin (Ubq), and the B3 domain of Protein G (GB3) were performed using Desmond version 2.1.0.1 and the Amber ff99SB or the modified Amber ff99SB-ILDN force fields. The TIP3P water model20 was used for simulations of HEWL, Ubq, and GB3, and the TIP4P-Ew water model21 (link) was used for simulations of BPTI. Simulation parameters were the same as in the simulations of small helical peptides, apart from the fact that a 643 PME grid was used for HEWL and a 483 grid was used for BPTI, Ubq, and GB3. Simulations of HEWL, BPTI, Ubq, and GB3 were initiated from PDB22 (link) entries 6LYT, 5PTI, 1UBQ, and 1P7E solvated in cubic water boxes containing 10,594, 4215, 6080, and 5156 water molecules, respectively. The net charge of the proteins was neutralized with sodium or chloride ions. Each system was initially subject to energy minimization, followed by 1.2 ns of MD simulation in the NPT ensemble during which the temperature was increased linearly from 10 to 300 K, and position restraints on the backbone atoms were annealed from 1.0 to 0.0 kcal mol−1 Å−1. After this initial relaxation, each system was simulated for 6 ns in the NPT ensemble. The frame of this simulation with the volume closest to the average volume was selected as the starting conformation for a production run of 1.2 μs in the NVT ensemble. The trajectories obtained from the NVT runs were used for subsequent data analysis.
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Publication 2010
Amber Aprotinin Chlorides Cuboid Bone Helix (Snails) hen egg lysozyme Ions Peptides Protein Domain Proteins Reading Frames Sodium Ubiquitin Vertebral Column
All simulations used the C36 FF
for lipids16 (link),17 (link) and the CHARMM TIP3P water model.43 (link)−45 (link) To get better sampling and check the convergence, five independent
MD simulations were performed for each bilayer system using NAMD,
GROMACS, AMBER, and OpenMM. The simulation temperature was maintained
above the transition temperature of each bilayer: 300.0 (POPS), 303.15
(DOPC/POPC), 310.0 (POPE), and 323.15 K (DPPC/PSM). In addition, the
pressure was maintained at 1 bar. PBC were employed for all simulations,
and the particle mesh Ewald (PME) method30 (link) was used for long-range electrostatic interactions. The simulation
time step was set to 2 fs in conjunction with the SHAKE algorithm46 (link) to constrain the covalent bonds involving hydrogen
atoms for all programs except GROMACS in which the LINCS algorithm47 (link) was used. After the standard Membrane
Builder
minimization and equilibration steps, the production
run of each simulation was performed for 250 ns. The optimal parameters
were determined using the most recent version of each program (NAMD
2.9, GROMACS 5.0, AMBER14, and OpenMM 6.2), such that the use of previous
versions can cause some problems. For example, the semi-isotropic
pressure coupling method was not implemented until version 6.2 of
OpenMM. The individual simulation protocols that we tested for each
MD program are summarized in Table 1 and described in detail below.
Publication 2015
1,2-oleoylphosphatidylcholine 1-palmitoyl-2-oleoylphosphatidylethanolamine Amber Electrostatics Tremor
All metabolite reference standards underwent a two-step derivatization procedure. Therefore 1 mg of each standard was dissolved in a solution of 1 ml methanol:water:isopropanol (2.5:1:1 v/v). Then 10 μl of each standard solution were taken out and evaporated to dryness. First, methoximation was performed to inhibit the ring formation of reducing sugars, protecting also all other aldehydes and ketones. A solution of 40 mg/ml O-methylhydroxylamine hydrochloride, (CAS: [593-56-6]; Formula CH5NO.HCl; Sigma-Aldrich No. 226904 (98%)) in pyridine (99.99%) was prepared. The dried standards and 10 μl of the O-methylhydroxylamine reagent solution were mixed for 30 s in a vortex mixer and subsequently shaken for 90 minutes at 30°C. Afterwards, 90μl of N-methyl-N-trimethylsilyltrifluoroacetamide (MSTFA) with 1% trimethylchlorosilane (TMCS) (1 ml bottles, Pierce, Rockford IL) was added and shaken at 37°C for 30 min for trimethylsilylation of acidic protons to increase volatility of metabolites. A mixture of internal retention index (RI) markers was prepared using fatty acid methyl esters (FAME markers) of C8, C9, C10, C12, C14, C16, C18, C20, C22, C24, C26, C28 and C30 linear chain length, dissolved in chloroform at a concentration of 0.8 mg/ml (C8-C16) and 0.4 mg/ml (C18-C30). 2 μl of this RI mixture were added to the reagent solutions, transferred to 2 mL glass crimp amber autosampler vials. Data acquisition parameters are given in table 1. Subsequent to data processing using the instrument manufacturer’s software programs, spectra and retention indices were manually curated into the new Leco FiehnLib (359-008-100) or automatically transferred by Agilent to the new Agilent FiehnLib (G1676AA).
Publication 2009
Acids Aldehydes Amber Cardiac Arrest Chloroform Esters Fatty Acids Isopropyl Alcohol Ketones Methanol methoxyamine Protons pyridine Retention (Psychology) Sugars trimethylchlorosilane Volatility
Models of single ions interacting with one or more water molecules were built and minimized in vacuo. Because the potential energy of either a single isolated ion or a single isolated water molecule (with the rigid water models used) is zero, the potential energy of the combined system is equivalent to the binding energy. For the cations and the anions with a single water molecule, C2v structures and Cs structures, respectively, represent the global minimum structures. In addition to these basic geometries, various other ion−water structures were built (see Figures 1 and 2). In the figures, the indices include two numbers (e.g., x + y) which indicate the number of water molecules in the first and second hydration shells, respectively. Some of these indices have the letter h next to them, which refers to a halfway or mixed interaction of the water molecules with both the first and the second hydration shells. Unfortunately, because the default minimization algorithms in AMBER are unstable, dated, and limited, the sander program could not accurately minimize the structures with fixed water bond distances (i.e., SHAKE(171 )). Therefore, the energy minimization was performed with a home-built Perl script validated to match the AMBER energies.
Publication 2008
Amber Anions Cations Muscle Rigidity Tremor

Most recents protocols related to «Amber»

Not available on PMC !

Example 19

TABLE 37
Embodiments of lyophilized silk powders
Silk SolutionTreatmentSoluble
~60 kDa silk, 6% silk, pH = 7-8lyopholize and cut withno
blender
~60 kDa silk, 6% silk, pH = 10lyopholize and cut withno
blender
~25 kDa silk, 6% silk, pH = 7-8lyopholize and cut withyes
blender
~25 kDa silk, 6% silk, pH = 10lyopholize and cut withyes
blender

The above silk solutions were transformed to a silk powder through lyophilization to remove bulk water and chopping to small pieces with a blender. pH was adjusted with sodium hydroxide. Low molecular weight silk (−25 kDa) was soluble while high molecular weight silk (−60 kDa) was not.

The lyophilized silk powder can be advantageous for enhanced storage control ranging from 10 days to 10 years depending on storage and shipment conditions. The lyophilized silk powder can also be used as a raw ingredient in the pharmaceutical, medical, consumer, and electronic markets. Additionally, lyophilized silk powder can be re-suspended in water, HFIP, or an organic solution following storage to create silk solutions of varying concentrations, including higher concentration solutions than those produced initially.

In an embodiment, aqueous pure silk fibroin-based protein fragment solutions of the present disclosure comprising 1%, 3%, and 5% silk by weight were each dispensed into a 1.8 L Lyoguard trays, respectively. All 3 trays were placed in a 12 ft2 lyophilizer and a single run performed. The product was frozen with a shelf temperature of ≤−40° C. and held for 2 hours. The compositions were then lyophilized at a shelf temperature of −20° C., with a 3 hour ramp and held for 20 hours, and subsequently dried at a temperature of 30° C., with a 5 hour ramp and held for about 34 hours. Trays were removed and stored at ambient conditions until further processing. Each of the resultant lyophilized silk fragment compositions were able to dissolve in aqueous solvent and organic solvent to reconstitute silk fragment solutions between 0.1 wt % and 8 wt %. Heating and mixing were not required but were used to accelerate the dissolving rate. All solutions were shelf-stable at ambient conditions.

In an embodiment, an aqueous pure silk fibroin-based protein fragment solution of the present disclosure, fabricated using a method of the present disclosure with a 30 minute boil, has a molecular weight of about 57 kDa, a polydispersity of about 1.6, inorganic and organic residuals of less than 500 ppm, and a light amber color.

In an embodiment, an aqueous pure silk fibroin-based protein fragment solution of the present disclosure, fabricated using a method of the present disclosure with a 60 minute boil, has a molecular weight of about 25 kDa, a polydispersity of about 2.4, inorganic and organic residuals of less than 500 ppm, and a light amber color.

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Patent 2024
Amber ARID1A protein, human Dietary Fiber Fibroins Freeze Drying Freezing Furuncles Light Pharmaceutical Preparations Powder Proteins Silk Sodium Hydroxide Solvents
Not available on PMC !

Example 125

[Figure (not displayed)]

Methyl 4-((5-(benzyloxy)-2-methoxyphenyl)(ethyl)amino)butanoate (184). 5-(Benzyloxy)-N-ethyl-2-methoxyaniline (146) (0.681 g, 2.65 mmol), DIEA (0.92 mL, 5.3 mmol), and methyl 4-iodobutyrate (0.72 mL, 5.3 mmol) in DMF (5 mL) were stirred at 70° C. for 5 days. The reaction mixture was cooled to rt, diluted with EtOAc (60 mL), washed with water (4×50 mL), brine (75 mL), dried over Na2SO4 and evaporated. The residue was purified by chromatography on a silica gel column (2.5×30 cm bed, packed with CHCl3), eluant: 5% MeOH in CHCl3 to get compound 184 (0.72 g, 76%) as a dark amber oil.

Methyl 4-(ethyl(5-hydroxy-2-methoxyphenyl)amino)butanoate (186). Ester 184 (0.72 g, 2.0 mmol) was stirred under reflux with 6 mL of water and 6 mL of conc HCl for 1.5 hrs and then evaporated to dryness to give acid 185 as a brown gum. The crude acid was dissolved in 50 mL of methanol containing 1 drop (cat.) of methanesulfonic acid ant the solution was kept for 2 hrs at rt. After that the mixture was concentrated in vacuum and the residue was mixed with 20 mL of saturated NaHCO3. The product was extracted with EtOAc (3×40 mL). The extract was washed with brine (40 mL), dried over Na2SO4 and evaporated. The residue was purified by chromatography on a silica gel column (2.5×30 cm bed, packed with CHCl3), eluant: 5% MeOH in CHCl3 to get compound 186 (0.444 g, 83%) as a brown oil.

N-(6-(dimethylamino)-9-(4-(ethyl(4-methoxy-4-oxobutyl)amino)-2-hydroxy-5-methoxyphenyl)-3H-xanthen-3-ylidene)-N-methylmethanaminium chloride (187). To a stirred suspension of tetramethylrhodamine ketone 101 (0.234 g, 0.830 mmol) in 10 mL of dry chloroform was added oxalyl chloride (72 μL, 0.82 mmol) upon cooling to 0-5° C. The resulting red solution was stirred for 0.5 h at 5° C., and the solution of compound 186 (0.222 g, 0.831 mmol) in dry chloroform (5 mL) was introduced. The reaction was allowed to heat to rt, stirred for 72 h, diluted with CHCl3 (100 mL and washed with sat. NaHCO3 solution (2×30 mL) The organic layer was extracted with 5% HCl (3×25 mL). The combined acid extract was washed with CHCl3 (2×15 mL; discarded), saturated with sodium acetate and extracted with CHCl3 (5×30 mL). The extract was washed with brine (50 mL), dried over Na2SO4 and evaporated. The crude product was purified by chromatography on silica gel column (2×50 cm bed, packed with CHCl3/MeOH/AcOH/H2O (100:20:5:1)), eluant: CHCl3/MeOH/AcOH/H2O (100:20:5:1) to give the product 187 (0.138 g, 29%) as a purple solid.

4-((4-(6-(dimethylamino)-3-(dimethyliminio)-3H-xanthen-9-yl)-5-hydroxy-2-methoxyphenyl)(ethyl)amino)butanoate (188). Methyl ester 187 (0.136 g, 0.240 mmol) was dissolved in 5 mL of 1M KOH (5 mmol). The reaction mixture was kept at rt for 1.5 hrs and the acetic acid (1 mL) was added. The mixture was extracted with CHCl3 (4×30 mL), and combined extract was washed with brine (20 mL), filtered through the paper filter and. The crude product was purified by chromatography on silica gel column (2×50 cm bed, packed with MeCN/H2O (4:1)), eluant: MeCN/H2O/AcOH/(4:1:1) to give the product 188 (0.069 g, 98%) as a purple solid.

N-(6-(dimethylamino)-9-(4-((4-(2,5-dioxopyrrolidin-1-yloxy)-4-oxobutyl)(ethyl)amino)-2-hydroxy-5-methoxyphenyl)-3H-xanthen-3-ylidene)-N-methylmethanaminium chloride (189). To a solution of the acid 188 (69 mg, 0.12 mmol) in DMF (2 mL) and DIEA (58 μL, 0.33 mmol) was added N-hydroxysuccinimide trifluoroacetate (70 mg, 0.33 mmol). The reaction mixture was stirred for 30 min, diluted with chloroform (100 mL) and washed with water (5×50 mL), brine (50 mL), filtered through paper and concentrated in vacuum. The crude product was purified by precipitation from CHCl3 solution (5 mL) with ether (20 mL) to give compound 189 (55 mg, 67%) as a purple powder.

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Patent 2024
Acetic Acid Acids Amber Anabolism Bicarbonate, Sodium brine Chlorides Chloroform Chromatography Esters Ethyl Ether Hydroxyl Radical Ketones methanesulfonic acid Methanol N,N-diisopropylethylamine N-hydroxysuccinimide oxalyl chloride Powder Silica Gel Sodium Acetate tetramethylrhodamine Trifluoroacetate Vacuum

Example 1

TABLE 1
Composition of liquid, ready-to-use
parenteral formulations of carmustine
CompositionFormulation 1
Carmustine100 mg
Polysorbate 80 NFq.s to 1 mL
  • (a) 100 mg of carmustine was dissolved in sufficient quantity (q.s. to 1 mL) of polysorbate 80 NF surfactant, under inert (nitrogen) gas purging.
  • (b) The solution obtained in step (a) was aseptically filtered (sterile 0.22 micron filter) under inert (nitrogen) gas purging to obtain a sterile product.
  • (c) The solution obtained in step (b) was filled into a sterile amber coloured type-I glass vial.

The stability of the formulation was tested after 3 months of storage at 2-8° C. The results are provided in Table 2 below.

TABLE 2
Evaluation of liquid ready-to-use parenteral
formulations of carmustine
Stability data
3 months
TestInitial(2° C.-8° C.)
DescriptionClear pale yellowClear pale yellow
color solutioncolor solution
Assay101.50% 97.21% 
Related substances
Impurity A*0.20%1.80%
Any unspecified impurityBLD**BLD**
Total impurities0.20%1.80%
*Impurity A refers to 1,3-bis(2-chloroethyl)urea
*BLD: below limit of detection

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Patent 2024
Amber Biological Assay Carmustine Nitrogen Parenteral Nutrition Pharmaceutical Preparations Polysorbate 80 Sterility, Reproductive Surfactants Urea
Not available on PMC !

Example 7

65% coconut oil, 20% rice bran oil, 10% palm oil, 5% castor oil.

100% KOH, 5% KCl (KCl based on oils weight)

Semi hard translucent amber colored bars. 2.5 kg/cm2 a few days after unmolding. 1.5:1 dilution easily dispersed with water to form watery clear thin translucent liquid soap. Good lather and skin feel.

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Patent 2024
Amber Castor oil Fatty Acids Feelings Oil, Coconut Oils Palm Oil potassium soap Rice Bran Oil Skin Technique, Dilution
Not available on PMC !

Example 5

65% coconut oil, 20% rice bran oil, 10% palm oil, 5% castor oil.

100% KOH, 25% KCl (KCl based on oils weight)

Hard semi translucent light amber colored bars 4.5 kg/cm2 a few days after unmolding. Good lather and skin feel. 1.5:1 dilution easily dispersed and slightly thickened translucent to clear liquid soap.

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Patent 2024
ADRB2 protein, human Amber Castor oil Fatty Acids Feelings Light Oil, Coconut Oils Palm Oil potassium soap Rice Bran Oil Skin Technique, Dilution

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More about "Amber"

Amber, PubCompare.ai's cutting-edge AI platform, empowers researchers to streamline their workflows and enhance the reproducibility and accuracy of their studies.
This innovative solution enables users to effortlessly locate protocols from scientific literature, preprints, and patents, and provides advanced AI-driven comparisons to help identify the most suitable protocols and products for their specific needs.
Amber's technology simplifies the research process, incorporating features such as Whatman No. 1 filter paper, Methanol, Thermostat, No. 1 filter paper, Formic acid, Milli-Q system, Acetonitrile, AutoDock Tools, Acetone, and DMSO, among others.
These tools and reagents work in tandem with Amber's AI-powered capabilities to optimize workflows, improve efficiency, and ensure that researchers can make well-informed decisions throughout their studies.
By leveraging Amber, researchers can access a comprehensive database of protocols, compare them side-by-side, and select the most appropriate options for their research needs.
This not only saves time and effort but also enhances the reproducibility and accuracy of their findings, ultimately contributing to the advancement of scientific knowledge.
Amber's intuitive interface and user-friendly design make it accessible to researchers across disciplines, from novice to experienced.
With its seamless integration of cutting-edge technology and a wide range of supportive features, Amber is poised to transform the way researchers approach their work, streamlining the process and delivering reliable, high-quality results.