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- Mass spectrometry is an extremely versatile detection system for GC. However, interfacing an HPLC system to a mass spectrometer is a much more difficult task. Describe the major reasons why it is more difficult to combine HPLC with mass spectrometry than it is to combine GC with mass spectrometry.Describe with illustrations the observed peak for a chromatogram with the following tailing factors (TF): a. TF = 1b. TF > 1c. TF < 1What are the parameters that can be used for analytes identification and quantification using Cyclic Voltammetry, respectively?
- You obtained the following raw data when setting up a Bradford standard curve: BSA (mg/ml) Absorbancy 595nm 0 0.225 1 0.310 2 0.420 3 0.510 4 0.610 5 0.720 6 0.810 7 0.915 8 0.950 9 0.980 10 0.990 After blanking against a bradford-dH2O sample, the protein concentration of an unknown sample was determined using the same method and an absorbancy of 0.523 was obtained. Set up a standard curve, excluding outliers (experimental and statistical) and determine the protein concentration in the unknown sample in mg / ml (up to 3 significant figures).the efficiency of a chromatographic column improves the measure thata.increases the height of the theoretical dishesb.decreases the number of theoretical platesc.platform height is reducedd.None of the above Which option is correct And explainI extracted caffeine by using chloroform and magnesium sulfate to dehydrate the organic phase. I got crude caffeine just by solvent evaporation at room temperature. However, I wanted to conduct Raman spectroscopy measurements but I did not get the characteristic peaks. I think that it has to be whit chloroform presence. So I let the crude caffeine 24h at 65 degrees but still I did not get any peak. What can I use to rinse my crude caffeine extract to remove all chloroform molecules? Or what is wrong with my extraction?
- The following Rf values were computed from a normal phase chromatography experiment. Arrange them from most polar to least polar. I - 0.25 II - 0.84 III - 0.56 IV- 0.67 Group of answer choices II > IV > III > I I > III > IV > II I > II > III > IV IV > II > III > Ia) How does mass spectrometry identify organic compounds? b) Describe the use and function of Quadrupole Analyzers ? c) One of the ionization sources for atomic mass spectrometry (MS) is Inductively Coupled Plasma (ICP). Explain the need for an interface in the ICPMS instrument and how can it be achieved.1. Describe the different types of analytes which can be analyzed using the different methods of optical analyses. 2. Why is it that absorbance readings be done at lambda max?
- The following data were obtained from a Bradford assay to determine the protein content in a sample: Protein content (μg) Absorbance value 0 0.000 2 0.022 5 0.065 10 0.106 20 0.178 30 0.299 40 0.380 50 0.472 unknown 0.150 a. use excel, another program, or graph paper to produce a calibration curve based on the data. b. Use linear regression (best fit line) to obtain the slope of the line c. Determine the unknown protein content for a sample that shows an absorbance reading of 0.150.Calculate the concentration of a solution of peptide AWSME, in mM if the absorbance at 280 nm for the solution is 0.6 absorbance units, and a 0.2-cm cuvette is used. For the extinction coefficient, take into account that e280(Trp) = 5690 M-1 cm-1 and e280(Tyr) = 1280 M-1 cm-1. Round your answer to two decimals.In a thin layer chromatography experiment, a plate of length 8.67 cm was used and a horizontal line was made at 1.11 cm above the bottom of the plate. After running the experiment (developing and drying), a spot was observed at 4.59 cm from the bottom of the plate, and the solvent front was 7.56 cm from the bottom of the plate. What is the Rf value?