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Sulfate

Sulfate is a chemical compound consisting of one sulfur atom bonded to four oxygen atoms.
It is an important anion found in various biological and environmental contexts, playing crucial roles in many metabolic processes.
Sulfate can be derived from the oxidation of sulfur-containing compounds and is involved in the regulation of fluid balance, bone development, and detoxification pathways.
Researchers studying sulfate-related processes may utilize PubCompare.ai's AI-driven protocol comparison tool to efficiently locate the best research protocols from literature, preprints, and patents, ensuring reproducible and accurate findings.
This comprehensive resource helps explore the latest sulfate-related research with ease and confidence, aiding in the advancement of our understanding of this essential chemical specie.

Most cited protocols related to «Sulfate»

1
Optimizing Photoautotrophic Cultivation of Chlorella
Cited 6 times
In order to study the influence of operational factors on photoautotrophic cultivation of C. sorokiniana for accelerated growth and biomass production, microalga with an initial OD750 of 0.01 (optical density at 750 nm) was grown in a sterilized 3.6 L Labfors 4 Lux photobioreactor (Infors HT, Bottmingen, Switzerland) with a 2.4 L working volume with controlled luminous flux levels. The experiments were divided into three main groups: (1) cultivation under different photosynthetic photon flux density (PPFD) conditions, (2) cultivation at various levels of carbon dioxide, and (3) cultivation in the presence of various levels of nitrate and sulfate ions.
The photobioreactor was illuminated with 1–16 Gro-Lux tubes with high blue and red radiation (per tube: 120 lumen (lm), maximum: 1920 lm) uniformly distributed around the culture vessel. Light intensity was additionally measured using a photosynthetically active radiation meter (PAR meter, Apogee Instruments, Logan, UT, USA). In experiments on the selection of optimal lighting, we tested the growth of culture at different values of illumination. Three treatments were carried out under different PPFD conditions (1000, 1200, and 1400 μmol m−2 s−1). For an optimized strategy for the growth and the accumulation of biomass, we analyzed the following conditions of the carbon dioxide regimen: cultures sparged with atmospheric air only (~0.04% CO2) and cultures sparged simultaneously with atmospheric air and continuously added CO2 (finally 0.5%, 1.0%, and 2.0% CO2 (v/v)). Aeration (0.55 volume of air per volume of liquid per minute) was provided by a compressor via a 0.45 µm filter. Carbon dioxide addition was provided by thermal mass flow meter and controller (Vögtlin Instruments, Aesch, Switzerland). They were mixed and injected into the reactor. The temperature was controlled at +26–26.5 °C. A relatively low temperature was chosen in our experiments since high temperatures lead to higher control costs and higher energy consumption of the process. The reactor was continuously stirred at 120 rpm. In all experiments, light was maintained on a 16:8 light/dark cycle. When observing the foam, a sterile 2% v/v solution of antifoam (Antifoam B, Sigma-Aldrich, St. Louis, MO, USA) was added. The experiments continued in the range of 112–232 h. Light, temperature, medium pH, pressure inside the reactor, carbon dioxide flow, and the percentage of released oxygen and carbon dioxide were measured by the Infors devices and displayed online on a computer screen.
Samples for analysis of algal growth, cell number, pigment content, and ions concentration in the culture medium were collected every day. pH as well percentage of the released molecular oxygen and carbon dioxide were measured throughout the experiments. Two independent experiments were performed to test reproducibility, and the results are presented as the mean.
Ziganshina E.E., Bulynina S.S, & Ziganshin A.M. (2020). Comparison of the Photoautotrophic Growth Regimens of Chlorella sorokiniana in a Photobioreactor for Enhanced Biomass Productivity. Biology, 9(7), 169.
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Publication 2020
Blood Vessel Carbon dioxide Cold Temperature Culture Media Fever Flowmeters Ions Light Lighting lumin Medical Devices Nitrates Oxygen Photobioreactors Photosynthesis Pigmentation Pressure Radiation Sterility, Reproductive Sulfate Treatment Protocols Vision
2
Lipid Extraction and Mass Spectrometric Analysis
Cited 6 times
Lipids were extracted from membrane fractions with chloroform/methanol/HCl (50:100:1.5, vol/vol/vol), as described by Bligh and Dyer 1959. Using a gentle stream of nitrogen, the organic phase was evaporated and the dried lipids were redissolved in chloroform/methanol (1:2, vol/vol). Phosphate determination was performed as described (Rouser et al. 1970), except that the assay volume was reduced by a factor of four. Glassware was used throughout the procedures.
MS was done on a QII triple quadrupole instrument (Micromass) equipped with a nano-ESI source. Nitrogen was used as a drying gas. The source temperature was set to 30°C. A capillary voltage of ± 600–800 V was applied, depending on the ion mode. Argon was used as collision gas at a nominal pressure of 3 × 10−3 mbar. Resolution of Q1 and Q3 was set to achieve isotope resolution. A collision energy of 30 eV was used for PC and SM detection in positive PREC mode, selecting a fragment ion of mass/charge (m/z) 184 (phosphocholine ion). Detection of cholesterol as cholesterol sulfate was done in negative PREC mode, selecting for a fragment ion of m/z 97 (sulfate ion) at a collision energy of 62 eV (Sandhoff et al. 1999). The mass range m/z scanned was 600–1,000 for PC and SM detection and 450–480 for cholesterol sulfate detection. For each quantitative measurement, 100 (PC and SM) or 50 (cholesterol) consecutive scans of 4-s duration were averaged.
PC and SM quantification was done as described (Brügger et al. 1997). 1,2-O-dilauroyl-sn-glycero-3-phosphocholine, 1,2-O-dimyristoyl-sn-glycero-3-phosphocholine, 1,2-O-diarachidoyl-sn-glycero-3-phosphocholine, and 1,2-O-dibehenoyl-sn-glycero-3-phosphocholine, as well as N-myristoyl-SM, N-oleoyl-SM, and N-pentacosanoyl-SM were used as standards. In brief, PC and SM standards dissolved in chloroform/methanol (1:2, vol/vol) were added to the extraction solvent before lipid extraction of membrane fractions. Dried lipids were redissolved in chloroform/methanol (1:2, vol/vol). Ammonium acetate (100-mM stock solution in methanol) was added to a final concentration of 5 mM to acidify the solution. Before mass spectrometric analysis, samples were spun at 15,000 gav for 5 min at 4°C in a microfuge (Eppendorf). Nano flow borosilicate glass tips of type D (Teer Coatings) were used. Instrument parameters were set as described above. For quantitative analysis, mass correction and isotope correction for [M+1], [M+2], and [M+3] isotopes were performed. Quantification of cholesterol was performed as described previously (Sandhoff et al. 1999).
Brügger B., Sandhoff R., Wegehingel S., Gorgas K., Malsam J., Helms J.B., Lehmann W.D., Nickel W, & Wieland F.T. (2000). Evidence for Segregation of Sphingomyelin and Cholesterol during Formation of Copi-Coated Vesicles. The Journal of Cell Biology, 151(3), 507-518.
Publication 2000
ammonium acetate Argon Biological Assay Capillaries Chloroform Cholesterol cholesteryl sulfate factor A Glycerylphosphorylcholine Isotopes Lipids Mass Spectrometry Membrane Lipids Methanol Nitrogen Phosphates Phosphorylcholine Pressure Radionuclide Imaging Solvents Sulfate Tissue, Membrane
3
Elemental Composition and Growth Reactions of SARS-CoV-2 Variants
Cited 4 times

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Publication 2022
Amino Acids Amino Acids, Acidic Amino Acid Sequence Bacteria Base Sequence Buffers Carbon Cell Nucleus Fungi Genome Ion, Bicarbonate Ions Nitrogen Nucleocapsid Nucleotides Nutrients Oxidants Oxygen Phosphoproteins Phosphorus Plants Proteins Reproduction SARS-CoV-2 spike protein, SARS-CoV-2 Strains Sulfate Sulfur Viral Components Virion Virus
4
Anaerobic Kinetics of Sulfate-Reducing Bacteria
Cited 4 times
The kinetics were investigated in sealed 250 mL glass bottles in which an equal amount of 200 mL of the previously autoclaved medium, without agar, and 50 mL of inoculum were added and put inside the anaerobic chamber. Then the bottles were continuously mixed in a mechanical shaker at 120 RPM at 38 °C. At certain time intervals, one bottle was selected, aliquots withdrawn and used for the chemical and biological analysis. The amount of Na2SO4 and FeSO4·7H2O of the modified Postgate medium were proportionately modified in the culture medium to reach the concentrations of 1790 mg/L; the amount of the other components of the culture medium was the same.
During the kinetic experiment samples were withdrawn at suitable time intervals and then after acidification the biomass concentrations are evaluated using the calibration curve in Fig. 1. The sulfate and sulfide solution content was measured by turbidimetric methods. Barium sulfate was added to the samples to precipitate the sulfate ions as barium sulfate and copper sulfate was added to precipitate the sulfide ions as copper sulfide. For the pH measurements a pH meter calibrated using buffer solutions of pHs of 4 and 7 was used. The redox potentials were measured using an ORP electrode with an internal Ag/AgCl reference electrode [1] , [2] .
Bernardez L.A, & de Andrade Lima L.R. (2015). Improved method for enumerating sulfate-reducing bacteria using optical density. MethodsX, 2, 249-255.
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Publication 2015
Agar Biopharmaceuticals Buffers Copper Culture Media Ions Kinetics Oxidation-Reduction Sulfate Sulfate, Barium Sulfate, Copper Sulfates, Inorganic Sulfides Turbidimetry
5
Structural Insights into H. pylori ClpX
Cited 4 times

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Publication 2009
AAA Domain Binding Sites Complement Factor B Crystallography Electrons factor A Helicobacter pylori Human Body Microtubule-Associated Proteins Muscle Rigidity Nucleotides Protein Subunits Sulfate

Most recents protocols related to «Sulfate»

1
Comprehensive Analysis of Water and Soil Quality
Sampling
locations were determined with the help of GPS coordinates (GARMIN
GPS eTrex 30x) surrounding Kirazlı village. Water and soil samples
were collected during the dry season (on September 6–7, 2019).
Water samples, including surface water (n = 3, nos.:
W11 (dam water), W2, and W32 (stream water)) and groundwater (n = 42, nos. 1–45, apart from W11, W2, and W32),
were collected in polyethylene bottles (500 mL), with the following
sampling and analytical procedure carried out using the Standard Methods
for the Examination of Water and Wastewater.45 Electrical conductivity (EC), total dissolved solid (TDS), dissolved
oxygen (DO), and pH were measured on-site. Additionally, total alkalinity,
sulfate ion (SO42–), and metal analysis
were conducted at the laboratory of the Environmental Engineering
Department of Gebze Technical University. The metals investigated
within the scope of this study were selected by taking into account
the metals and metalloids in the soil and water samples as a result
of the preliminary analysis by an inductively coupled plasma-optical
emission spectrophotometer (ICP-OES, Optima 7000 DV, PerkinElmer).
As a result of the preanalysis, metals such as As, Cr, Hg, and V were
not detected in the samples; therefore, these metals were not considered
in the study. Consequently, total concentrations of 15 metals (Al,
B, Ba, Ca, Cd, Co, Cr, Cu, Fe, Mg, Mn, Ni, Pb, Si, and Zn) were analyzed
by ICP-OES.
Each of the surface soil samples (∼500 g)
was collected from close to the springs at 0–10 cm (upper soil
layer) soil samples (n = 12 S1–S12) and collected
into polyethylene bags. All samples were transferred to the laboratory
and stored at 4 °C. Before being ground to <100 μm with
a mortar, the soil samples were dried at 105 ± 2 °C for
48 h. Then, 0.25 g of sample was exposed to 2 mL of HNO3, 2 mL of HF, 1 mL of HCl, and 1 mL of H2O2 in Teflon vessels for 24 min and digested in a model Milestone Ethos
1600 advanced microwave digestion apparatus. Then, each digestate
was diluted to 50 mL with ultrapure water, and the resulting solution
was analyzed for the 15 metals with the water samples by ICP-OES.
All reagents used were of analytical grade. X-ray diffraction (XRD,
Bruker D-8 Advance) was applied for mineralogical identifications
on randomly collected soil samples. The identification was also supported
by scanning electron microscopy (SEM, Philips XL 30S-FEG, The Netherlands)
equipped with energy-dispersive X-ray spectroscopy (EDS, AMETEK Inc.).
Hızlı S., Karaoğlu A.G., Gören A.Y, & Kobya M. (2023). Identifying Geogenic and Anthropogenic Aluminum Pollution on Different Spatial Distributions and Removal of Natural Waters and Soil in Çanakkale, Turkey. ACS Omega, 8(9), 8557-8568.
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Publication 2023
Alkalies Blood Vessel Digestion Electric Conductivity Energy Dispersive X Ray Spectroscopy Metalloids Metals Microwaves Natural Springs Peroxide, Hydrogen Plasma Polyethylene Scanning Electron Microscopy Sulfate Teflon X-Ray Diffraction
2
Crystallographic Structure Determination of Aim Proteins
Crystallization experiments and structure determination were conducted in the Collaborative Crystallography Core in the Department of Biochemistry at the University of Wisconsin. All crystallization screens and optimizations were conducted at 293K in MRC SD-2 crystallization plates, set with a STP Labtech Mosquito crystallization robot. Hampton IndexHT and Molecular Dimensions JCSG+ were used as general screens. Crystals were cooled by direct immersion in liquid nitrogen after cryopreservation and harvest using MiTeGen MicroMounts. X-ray experiments were conducted at the Advanced Photon Source, Argonne National Lab, GMCA@APS beamline 23ID-D. Diffraction data were collected on a Pilatus 3-6M detector and reduced using XDS (79 (link)) and XSCALE (80 (link)). Structure solution and refinement used the Phenix suite of crystallography programs (81 ). Iterative rounds of map fitting in Coot (82 (link)) and phenix.refine (83 (link)) were used to improve the atomic models. MOLPROBITY (84 (link)) was used to validate the structures. Data collection and refinement statistics for the structures can be found in Table S3.
The best crystals of SeMet Aim18p-Nd70-R123A grew from 26% PEG 3350, 0.2 M Li2SO4, 0.1 M Na-Hepes buffer, pH 7.5. Crystals were cryopreserved by supplementing the PEG concentration to 30%. Diffraction data extending to 2.2 Å was collected on 2018-02-07 at energies near the SeK-edge (peak = 0.97937 Å, edge = 0.97961 Å, and high remote at 0.96437 Å). Phenix.hyss (85 (link)) located the expected 5 Se sites from one copy of the protein per asymmetric unit in space group P3221. The structure was phased and traced using Phenix.autosol (86 (link)) with a phasing figure of merit = 0.47 and map skew = 0.6. The initial chain trace was continuous from residue 88 to the C-terminus. The final model starts at residue 83 and includes five sulfate ions per chain.
The best crystals of Aim46p-FL-WT were grown using microseeds obtained from a similar condition. The seeds were stabilized in 30% PEG 2000, 0.1 M MES pH 6.5. The droplet was composed of 20 nl microseed suspension, 180 nl Aim46p-Nd62-WT, and 300 nl PEG 2000, 0.1 M MES, pH 6.5. Crystals were cryoprotected with 30% PEG 2000. Data were collected on 2018-12-08 at 1.0332 Å. Data extended to 2.0 Å and belonged to space group P21. One copy of the protein per asymmetric unit was by molecular replacement using Phaser starting from an appropriately pruned Aim18p-Nd70-R123A model (log-likelihood gain 307, translation function z-score 11.7). The final model is continuous from residue 70 to the C-terminus and includes a ligand modeled as α-ketoglutarate.
Schmitz J.M., Wolters J.F., Murray N.H., Guerra R.M., Bingman C.A., Hittinger C.T, & Pagliarini D.J. (2023). Aim18p and Aim46p are chalcone isomerase domain–containing mitochondrial hemoproteins in Saccharomyces cerevisiae. The Journal of Biological Chemistry, 299(3), 102981.
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Publication 2023
alpha-Ketoglutaric Acid Buffers Crystallization Crystallography Culicidae HEPES Ligands Nitrogen Plant Embryos polyethylene glycol 3350 Proteins Radiography Submersion Sulfate
3
Structural Refinement of V-ATPase
Maps from DeepEMhancer were used for model building, refinement, and subsequent structural interpretation. The V1EG model of the V/A-ATPase was adopted from the 3.1 Å V1EG structure (PDB accession no. 7VAL) as the initial model (23 (link)). With 2.5 to 3.1 Å V1EG density maps, we could model side chains and local geometry to achieve higher accuracy (Fig. S7A). The initial model was docked into the cryo-EM map using UCSF ChimeraX (42 (link)), and sulfate ions were built into COOT (43 (link)), followed by several rounds of real-space refinement using Phenix (44 (link), 45 (link)). The initial model manually corrected residue by residue in COOT (43 (link)) regarding side-chain conformations. The iterative process using COOT (43 (link)) and ISOLDE (46 (link)) was performed for several rounds to correct the remaining errors until the model agreed well with the geometry (Table S2). Cross-validation was carried out by comprehensive validation in Phenix (44 (link), 45 (link)), and the map to model Fourier shell correlation curves was calculated (Fig. S7B). Root means square displacement values between the atomic models and structural figures were calculated using the UCSF chimeraX (42 (link)).
Nakanishi A., Kishikawa J.I., Mitsuoka K, & Yokoyama K. (2023). Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding. The Journal of Biological Chemistry, 299(2), 102884.
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Publication 2023
Adenosinetriphosphatase MAP2 protein, human Microtubule-Associated Proteins Plant Roots Sulfate
4
Banana Peel-Supported Sulfonic Acid Catalysts
Four batches of banana peel-supported sulfonic acid (BP-SO3H) catalysts were prepared by varying the banana peel-to-sulfuric acid ratio, reaction time, and temperature. Catalysts prepared in the initial batch include dried banana peel powder (1 g) mixed thoroughly with conc. H2SO4. Banana peel powder: H2SO4 ratios (g L−1) of 1:5, 1:10, 1:15, and 1:20 were used, whereas the reaction temperature varied between 80 and 120 °C while reaction time was monitored for 16, 18, 20, 22, and 24 h. In order to remove residual sulfate ions in the filtrate, 50–60 mL of deionized water was added to the mixture. It was washed several times with hot deionized water until no residual sulfate ions could be detected (a 6 mol L−1 solution of BaCl2 was used for testing). The resultant sulfonic acid functionalized banana peel (BP-SO3H) was dried in an oven overnight. All the synthesized BP-SO3H catalysts were assigned a code based on their synthesis procedure; BP-SO3H-X-Y-Z, where X is the wt/volume ratio of banana peel/H2SO4, Y is the 'in 'situ' hydrothermal-sulfonation time, and Z stands for reaction temperature. Accordingly, the catalyst prepared using a 1:10 (wt/volume) banana peel/sulfuric acid ratio, hydrothermal sulfonation time of 16 h, and reaction temperature of 80 °C were designated as BP-SO3H-10-16-80.
Devasan R., Ruatpuia J.V., Gouda S.P., Kodgire P., Basumatary S., Halder G, & Rokhum S.L. (2023). Microwave-assisted biodiesel production using bio-waste catalyst and process optimization using response surface methodology and kinetic study. Scientific Reports, 13, 2570.
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Publication 2023
Anabolism Banana barium chloride BP 16 Powder Sulfate Sulfonic Acids Sulfuric Acids
5
Molecular Dynamics Simulations of Chorismate Mutase
Molecular dynamics (MD)
simulations were carried out on a number of representative structures
for CM. They included two independent sets of simulations for apo
MtCM, starting either from the X-ray crystal structure of MtCM in
complex with malate (after removing malate) (PDB ID: 2VKL)21 (link) or from the structure of the CM polypeptide in the apo
MtCM–MtDS complex (PDB ID: 2W19,21 (link) chain D).
The malate complex was chosen over ligand-free MtCM (PDB ID: 2QBV)41 (link) due to its higher resolution and better refinement statistics.
Both simulations gave essentially the same result; therefore, we will
not refer to the second data set any further. For the highly active
evolved MtCM variant (MtCMV), we used the recent crystal
structure (PDB ID: 5MPV).12 (link) The MtCM–ligand complex (MtCMLC) was taken from PDB ID: 2W1A,21 (link) excluding
the MtDS partner protein, where MtCM was co-crystallized with a transition
state analog (TSA) in its active site (Figure 1). Finally, the V55D variant was modeled
based on a partially refined experimental structure (Table S1). Residues that were not fully defined were added
to the models using (often weak) electron density maps as reference
in Coot.37 (link) When no interpretable
density was visible, geometric restraints (and α-helical restraints
for residues in helix H1) were applied during model building, to ensure
stable starting geometries. The N-termini of all of the models were
set at Glu13, corresponding to the first defined residue in almost
all of the resolved structures available. Glu13 was capped with an
acetyl group to imply the continuation of the H1 helix. CM dimers
were generated by 2-fold crystallographic symmetry.
Missing
H-atoms were added to the model and the systems were solvated in a
periodic box filled with explicit water molecules, retaining neighboring
crystallographic waters, and keeping the protein at least 12 Å
from the box boundaries. The systems were neutralized through the
addition of Cl– ions at a minimum distance of 7
Å from the protein and each other. Additional buffering moieties
like glycerol or sulfate ions found in the crystals were not considered.
MD simulations were run using the Gromacs 5.1.4 package42 (link),43 (link) using the AMBER 12 force fields for the protein moieties44 (link),45 and the TIP3P model for water.46 (link) The
ligand was modeled using the GAFF force field.47 (link) The smooth particle mesh Ewald method was used to compute
long-range electrostatic interactions,48 (link) while a cutoff of 11 Å was used to treat the Lennard–Jones
potential.
The systems were minimized using the steepest descent/conjugate
gradients algorithms for 500/1500 steps until the maximum force was
less than 1000 kJ mol–1 nm–1.
To equilibrate and heat the systems, first we ran 100 ps MD in the
NVT ensemble starting from a temperature of 10 K, using the canonical
velocity rescaling thermostat49 (link) followed
by 100 ps in the NpT ensemble with a Parrinello–Rahman barostat50 (link) targeting a final temperature of 310 K and a
pressure of 1 atm. After initial equilibration, 1 μs of MD simulation
was performed for each system. In all MD simulations, the time step
size was set to 2 fs.
Thorbjørnsrud H.V., Bressan L., Khatanbaatar T., Carrer M., Würth-Roderer K., Cordara G., Kast P., Cascella M, & Krengel U. (2023). What Drives Chorismate Mutase to Top Performance? Insights from a Combined In Silico and In Vitro Study. Biochemistry, 62(3), 782-796.
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Publication 2023
Amber Crystallography Debility Electrons Electrostatics Glycerin Helix (Snails) Ions Ligands malate Metatropic dwarfism Microtubule-Associated Proteins Molecular Dynamics Polypeptides Proteins Radiography STEEP1 protein, human Sulfate

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More about "Sulfate"

Sulfur-containing Compounds, Sulfur Oxidation, Fluid Balance, Bone Development, Detoxification, Sulfur Metabolism, Sulfur Redox Reactions, Sulfur Cycle, Sulfur-Oxidizing Bacteria, Sulfur Amino Acids, Sulfur Assimilation, Sulfur Dioxide, Sulfuric Acid, Sulfate Esters, Sulfated Glycosaminoglycans, Sulfotransferases, Sulfate-Reducing Bacteria, Sulfur Isotopes, Sulfur Speciation, Sulfur Mineralization, Sulfur Compounds in Plants, Sulfur Compounds in Animals, Sulfur Compounds in Microorganisms, Sulfur Compounds in the Environment, Sulfur Compounds in Industry, Sulfur Compounds in Medicine, Sulfur Compounds in Agriculture, Sulfur Compounds in Food, Sulfur Compounds in Fuels, Sulfur Compounds in Pollution, Sulfur Compounds in Biochemistry, Sulfur Compounds in Geochemistry, Sulfur Compounds in Analytical Chemistry, Sulfur Compounds in Organic Chemistry, Sulfur Compounds in Inorganic Chemistry, Sulfur Compounds in Bioinorganic Chemistry, Sulfur Compounds in Medicinal Chemistry, Sulfur Compounds in Environmental Chemistry, Sulfur Compounds in Materials Science, Sulfur Compounds in Catalysis, Sulfur Compounds in Spectroscopy, Sulfur Compounds in Mass Spectrometry, Sulfur Compounds in Nuclear Magnetic Resonance, Sulfur Compounds in X-ray Crystallography, Sulfur Compounds in Molecular Modeling, Sulfur Compounds in Biophysics, Sulfur Compounds in Structural Biology, Sulfur Compounds in Enzymology, Sulfur Compounds in Metabolomics, Sulfur Compounds in Proteomics, Sulfur Compounds in Lipidomics, Sulfur Compounds in Glycomics, Sulfur Compounds in Bioinformatics, Sulfur Compounds in Systems Biology, Sulfur Compounds in Pharmacology, Sulfur Compounds in Toxicology, Sulfur Compounds in Drug Discovery, Sulfur Compounds in Biomedical Research, Sulfur Compounds in Environmental Science, Sulfur Compounds in Agricultural Science, Sulfur Compounds in Food Science, Sulfur Compounds in Materials Engineering, Sulfur Compounds in Chemical Engineering, Sulfur Compounds in Process Engineering, 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