None The accurate mass of the monoisotopic peak for a peptidewas measuredusing MALDI to be 804.068 Da, while the exact mass for thepeptide wascalculated to be 804.073 Da. Determine the mass error inppm and brieflyexplain the significance of the mass error in enabling ascientist to identifythe peptide.

Significance of the Mass ErrorThe mass error in ppm is a crucial parameter in mass spectrometry as…

Answered: The accurate mass of the monoisotopic…

Fundamentals Of Analytical Chemistry

9th Edition

ISBN:9781285640686

Author:Skoog

Publisher:Skoog

Chapter33: High-performance Liquid Chromatography

Section: Chapter Questions

Problem 33.12QAP

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A protein consists of two types of peptide chains (A and B) with an unknown stoichiometry (AxBy). When you ran this protein directly on reversed phase-HPLC with UV monitor set at 280 nm, two peaks were resolved. Mass spec determined that the peaks represented Chain A and Chain B, respectively. The peak area is 500,000 for Peak A (Chain A) and 100,000 for Peak B (Chain B). The molecular masses of Chain A and Chain B are 25,000 and 5000, respectively. The extinction coefficients for Chain A and Chain B are 1 mL/mg.cm and 0.5 mL/mg.cm, respectively. Please calculate x/y.
The molecular weight of horse myoglobin is 16,951.49 Daltons. Intact proteins analysed by ESI-MS exhibits multiple charges distribution.a. Calculate the expected m/z [M+15H]15+ ion of the horse myoglobinb. If you were to identity the myoglobin protein by ESI-MS from across differentspecies, and you observe the ion m/z 1,413.6241, would you identify it as the horsemyoglobin or the sperm whale myoglobin (17,199.91 Da)?
In a Bradford assay, 17 pl of a protein isolate sample was diluted by adding 24 pl of water prior to the addition 2.0 mL Bradford reagent, Calculate the protein concentration (in mg/ml) of the original protein isolate sample whose absorbance reading at 595 nm is 0,384 after dilution The protein standard solutions used for the calibration curve of the Bradford assay was constructed using bovine serum albumin (BSA) stock solution whose concentration is 200 ug/mL The concentration and the corresponding absorbance reading at 595 nm of the protein standard solutions are summarized in the table below: Standard soln # 3 6 conc of BSA Kug/mL) 12.00 24.00 36.00 48.00 60.00 Absorbance lat 595 nm 0.000 0.156 0.249 0.328 0.411 0.528 zNote: Final answer format must be x.xox (three decimal places) Round off only in the final answer. Do not round off in the middle of the calculation
Based on the chromatograms, Symmetry C18 (top) is less selective than Symmetry Shield RP18 (bottom) for the analytes given, true or false?
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.
3. (a) The following are the results from subjecting the lectin to SDS-PAGE: Band / Molecular Length 210 100 67 48 32 Lectin Weight (kDa) of Gel Migration Distance 7.2 1.8 2.5 3.2 3.9 4.7 3.5 (cm) Determine the molecular weight of the lectin. Show all workings.
The negative ion mode electrospray ionization (ESI) mass spectrum of an oligonucleotide shows peaks at the following m/z ratios: 2903.8 (40%), 2580.9 (67%) , 2323.7 ( 100 % ) , 2111.4 (71%), and 1935.7 (38%). What is the molecular weight of this molecule? Please show your calculations and use all peaks to determine significant figures.
In a mixture of the five proteins listed below, which should elute second in size- exclusion (gel- filtration) chromatography? A) cytochrome c B) ribonuclease A C) immunoglobulin G D) RNA polymerase E) serum albumin M. = 13,000 Da M. = 13,700 Da M. = 145,000 Da M. = 450,000 Da M. = 68,500 Da
Determine the isotopic peak scheme for [ReCl]+ fragment in the mass spectrum? 185Re: %37 ; 187Re: %63; 35Cl: %76; 37Cl: %24
The standard curve of a biuret assay gave the equation: y=0.4193x. The absorbance for Unknown A = 0.098 and Unknown B = 0.325. Are you equally confident in the accuracy of the protein %D concentrations you would calculate for samples Unknown A and Unknown B? Briefly explain your answer.
In order to improve the peptide separation by using a HPLC system, trifluoroacetic acid acts as mobile-phase modifier was added during the preparation of mobile phase. The preparation was performed by a postgraduate student as following:“2.851 g trifluoroacetic acid (MW: 114.02 g/mol) was made up to 500 cm3 in a graduated flask. To this solution, 50 cm3 of ethanol was added, and after mixing the mobile phase was placed in the solvent reservoir and pumping was commenced at 1.5 cm3 min-1.”Based on the given preparation procedure, identify THREE mistakes that were made.
The Bradford method described in the Background section was used to determine protein concentrations of known and unknown samples The following results was obtained: Table 1: Absorbance at 595nm obtained for different concentrations of protein standards using the Bradford method Protein (mg/ml) 0.00 0.125 0.25 0.50 0.75 1.00 1.50 2.00 Unknown Abs. BSA 0 0.130 0.350 0.620 0.870 1.120 1.400 1.600 0.635 Abs. BIg 0 0.080 0.230 0.460 0.520 0.410 0.510 0.700 Calculate the concentration of the unknown protein in mg/ml

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