please solve question 13 Q11: Which ion chromatography conditions is suitable to isolate a protein that has a surface rich in Dand E amino acids?A) cation exchanger resin running at pH > plB) cation exchanger resin running at pH plD) anion exchanger resin running at pH

The different type of inhibition can be represented as follows: Graph A: Competitive inhibition; KM…

The graph below represents one of the enzymes inhibition mechanism, answer the following: A Y (C) L== 0 B +1 Slope = K(C) Vmax -1 Slope = KM Vmax X Q13) Which mode of inhibition does the graph represent? A) Pure competitive B) Mixed competitive C) Pure noncompetitive D) Uncompetitive E) Irreversible inhibition

The graph below represents one of the enzymes inhibition mechanism, answer the following: A Y (C) L== 0 B +1 Slope = K(C) Vmax -1 Slope = KM Vmax X Q13) Which mode of inhibition does the graph represent? A) Pure competitive B) Mixed competitive C) Pure noncompetitive D) Uncompetitive E) Irreversible inhibition

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.52P

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About a decade ago, it was more common to use peptide mass mapping to identify a protein cut from a gel. Peptide mass mapping involves digesting the protein with trypsin and then measuring the peptide masses using MALDI-TOF mass spectrometry. The more superior method of identifying a protein from a gel is to digest the protein with trypsin and then use liquid chromatography to separate the peptides. The separated peptides are then electrosprayed into a tandem mass spectrometer. The MS-MS data is uploaded into a database such as MASCOT for protein identification. Explain why the LC-MS-MS method is superior to the peptide mass mapping method.
+Protein Mr pl А 12,000 28,000 42,000 66,000 (a;) 103,000 (a2) 111,000 3 8.4 C 7.2 9 E 5 F 4.2 Predict how the proteins listed above will behave in a variety of separation and characterization procedures. For each chromatographic technique (you may assume that the protein remains “native," or non-denatured), list the order in which the proteins will elute (come of the end of the column): Size Exclusion Chromatography, pH 6.8 First Last Anion Exchange Chromatography, pH 9, using a salt gradient to elute First Last
One of the most advanced methods for determining a protein sequence is tandem mass spectrometry (MS/MS). Select from the list of statements below all that applies to MS/MS. Group of answer choices CID is one way of performing tandem MS experiments The experiment start by chopping the protein into smaller peptide fragments using an enzyme These peptide fragments are later introduced into the mass spectrometer to determine their molecular weight Peptide fragments are selected for further fragmentation by collision with an inert gas There are only 4 types of ions which can result from MS/MS fragmentation: a, b, x, and y ions The a and b ions are the ones with the original C terminus, whereas the x and y ions are the ones with the original N-terminus All of the above
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1. please do not worry about the table, answer the questions. thanks. 2.images You compare the proteins from blood samples from 2 siblings; one with blond hair and the other with black hair, by 2D gel electrophoresis. What method would you use to identify unique proteins on the gel. Why
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Of the following methods listed below, which could not be used to obtain a reasonable estimate of the molecular mass of a monomeric protein? Select all that apply. O Electrospray ionization mass spectrometrylsoelectric focusing O Gel filtration O All of these methods could be used O Isoelectric focusing O Sodium dodecyl sulfate polyacrylamide gel electrophoresis O Total amino acid sequence determination by Edman degradation
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Pre-Lab Questions 1. Define a protein, and describe one important function of proteins in the human body. 2. The following data were obtained from a Bradford assay to determine the protein content in a sample: Protein content (ug) 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 Use Excel, another program, or graph paper to produce a calibration curve based on the data. Use linear regression (or best fit line) to obtain the slope of the line. Determine the unknown protein content for a sample that shows an absorbance reading of b. С. 0.150.
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Question 32 Use the following chromatogram of standard amino acids: 24 11 16 19 3 12 21 15 6, 8 9 19 23 2 13 14 17 18 24 22 10 12 14 16 18 20 22 24 26 Time (min) Which of the following statements BEST describe the given chromatogram? O Peaks 4, 5, 11 and 24 have the highest concentrations in the mixture and highest affinity to the mobile phase. Peaks 14, 18, 20 and 22 have the lowest concentrations and highest affinity to the mobile phase. O The peaks are narrow and show clear separation of the mixture. The peaks are narrow and show suboptimal conditions for separation. (Au)
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