question 28 // both pictures are attached below. Each peak on the tandem mass spectrogram represents a product ion with a +1 charge. Use the spectrogram and the table ofamino acid masses to determine the amino acid sequence of the precursor peptide ion.4IntensityIArg100175.11200312.17300399.20400Mass/chargeO500546.27603.29600AlaAspGlyLeuPheThr700Answer BankArgGinHisLysProTrpValAsnGluIleMetSerTyr ResidueGlyAlaSerProValThrCysIleLeuAsnMass (Da)57.0271.0487.0397.0599.07101.05103.00113.08113.08114.04ResidueAspGlnLysGluMetHisPheArgTyrTrpMass (Da)115.03128.06128.09129.04131.05137.06147.07156.10163.06186.08

Mass spectrometry is an analytical gel-free proteomics method used for identification of proteins,…

Answered: Each peak on the tandem mass…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.
Look at the amino acid composition of a protein given in the table and click on the area in the 2D gel electrophoresis where you may expect the corresponding band. Amino acid composition M N P 7 3 11 A D E F G K R S V W Y ТОTAL: 16 2 12 14 4 1 3 7 2 11 11 10 1 164 Download Image. pH7 pH 9 pH3 200,000 116,250 97,400 66,200 45,000 31,000 21,500 14,400 ||| | |||
a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? Explain
The sequence of a peptide is given below. YGGFMTSEKSQTPLVTLFKNAIIKNAYKKGE If you perform peptide sequencing by tandem mass spectroscopy, calculate the predicted m/z ratio for b1, b5, b12, y1, y5 and y12 ions.
A mixture of five proteins are analyzed by MALDI-TOF. Their molecular weigths are 3 kD, 22 kD, 100 kD, 225 kD and 515 kD. A peak appears in the mass spectrum at 33.3 kD. Which protein most likely gave this peak?
Using mass spec, the primary structure of 4 peptides is obtained from a tissue sample: VMDEL, GHKRT, CNPQI, and SAWFY. The pI of each peptide is calculated and ion exchange chromatography is used to purify each peptide. VMDEL, GHKRT, CNPQI, and SAWFY were separated into 4 pure samples. The labels on all the samples are erased by mistake, and the mass spec is no longer working. You can run a few simple tests to identify the samples. What are 4 tests to identify each peptide and why?
Consider the following protein mixture: Protein A B C D Molecular Weight (kDa) 50 150 200 350 Affinity to Metal ion === Zn²+ === 1. Using hydrophobic interaction chromatography, the protein that will be eluted last is [Select] 2. Using affinity chromatography, the protein that will be eluted last in a Zn²+-containing column is 3. The protein with the fastest migration towards the anode in SDS-PAGE is [Select] IpH value 7 3 9 5 [Select] [Select] 4. Using a buffer solution with a pH of 4, the protein that will bind to an anion exchanger is 5. The protein that will be eluted last in a gel filtration column is [Select] 6. Using isoelectric focusing, the protein that will have a protein band nearest to the cathode (negative electrode) is [Select] % Hydrophobicity 20 45 75 55
Which of the peptide sequences below best matches the hydropathy plot shown? 5 10 15 Residue Number ILYYAGSREDHSGYLIL EQSDTERNQHGALIYLI LIFLAIFPAGSTSEDRR RAFLILFMTYFLILFLI LHGDQNRERDGHSQERD 2 Hydropathy value 0 -4 -2
The diffusivity of amino acids in polyacrylamide gel is approximately 1x10^-9 cm2./s calculate the initial flux of amino acids, give an instantaneous gradient of (20g/cm 3 )/8cm Why is polyacrylamide gel is used in electrophoresis?
An ion-exchange chromatographic separation is performed using a diethyl-aminoethyl- (DEAE)-sepharose column to separate proteins in a mixture. The mixture contains Protein A (pl=6.0), B (pl35.0), C (pl=7.5), D (pl =1), and E (pl=4.0). The protein mixture is prepared in a buffer solution pH =5. When the protein mixture is loaded onto the column, and the column is washed with a buffer solution pH 5, which protein(s) will be captured by DEAE-sepharose in the column? O Protein B because it is predominantly in net negative charge form. O Proteins D and E because they have predominately net negative charge in pH 5 solution O Proteins A, C, D and E because they have charges O Proteins A and C because both both predominantly have net positive charges O Proteins Band E because both predominantly have net positive charges
The A280 of a protein sample loaded onto a gel was determined to be 0.767 (1.00 cm path length, after subtracting the blank). The total volume of this sample was 428 µL. 19.0 µL of this protein sample was mixed with 19.0 µL of 2X laemalli sample buffer and then 12.0 µL of the entire sample was loaded into the gel and electrophoresed. Calculate the amount of protein that was loaded into the gel (in µg).
Complete the table below by adding (+) or (-) if eahc sample (amino acid or protein) below will test positive or negative, respectively. sample BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOSKIN-COLE G W H Y C R HAIR GELATIN CASEIN PEPTONE Identify the amino acid that will give the following data: BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOPSKIN-COLE - + + + - - + - Name of amino acid: structurte of the amino acid:

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