6. Consider the following proteins to answer the questions below:ProteinSize (kDa)plε at 280 nm104700050414000108300050850000AB CCRed Colored?YesNoNoNob. Describe a two-step purification procedure that could be used to purify/isolateprotein A from the other proteins. In your response, describe the type ofchromatography used, the pH of buffer needed, and a labeled chromatogram(include absorbances at both 280 and 400 nm). Make sure you note which"fraction/sample" is needed from the first step to proceed/use for the secondstep. Use another page if necessary.

Chromatography is a laboratory technique used to separate mixtures of different components. It works…

Answered: Describe a two-step purification…

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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Amino acid compositions can be determined by heating a protein in 6 M HCl and running the hydrolysate through an ion-exchange column. If you were going to do anamino acid sequencing experiment, why would you want to get anamino acid composition first?
pls explain Increasing the saturation of the ammonium sulfate is a prerequisite in isolating a target protein that is rich in Cys and Tyr residues. Which of the following techniques should be considered in accurately quantifying the isolated protein?I. Running the isolated protein in a dialysis or GFC set up.II. Using Biuret or BCA assay as the colorimetric quantitation method.III. Using Bradford or Lowry assay as the colorimetric quantitation method.A. I onlyB. II onlyC. I and IIID. I, II and III. Bradford Assay is most suitable to use when the extraction buffer is below the target protein’s pI. This is so because the protein would be morea. Positively charged allowing the CBB G-250 dye to bind via its sulfonate groups.b. Negatively charged allowing the CBB G-250 dye to bind via its sulfonate groups.c. Neutrally charged allowing the CBB G-250 dye to bind via its sulfonate groups.d. Zwitterionic allowing the CBB G-250 dye to bind via its sulfonate groups.
You want to isolate a protein which is thermally highly stable. This protein is currently in suspension in a liver homogenate. Give a detailed description of the preliminary fractionation process which you would use in the isolation of this protein.
A bioactive linear peptide was detected in amphibian toxıns. The peptide was found to be made up of 10 amino acids only, 2 of which are cysteines, 2 are arg, while the rest are either nonpolar or polar uncharged amino acids; no aromatic residues were also detected by amino acid analysis. The bioassay-guided isolation required the monitoring of the relative concentrations of proteins present. Which of the following quantitative and qualitative protein analysis will give a negative result? A. Lowry method B. Bradford method O C. Ultraviolet D. Bicinchoninic method E. Biuret
What are some advantages of sequencing peptides by mass spectrometry rather than by Edman degradation?
What is the purpose of a standard curve for a colorimetric enzyme assay?
Predict the amino acid sequence based on the conditions below. Use the one-letter abbreviation of amino acids. a. The amino acid in the C-terminal is optically inactive. b. The fifth amino acid is a neutral aromatic amino acid that yields a negative result for the Xanthoproteic test using intact protein while producing a yellow soln with Xanthoproteic reagent and yielding a negative result with Hopkin's Cole test using basic hydrolysate. c. Yields serine and a hexapeptide after treatment of aminopeptidase (specificity: peptide bond on the N-terminus). d. The amino acid beside the N-terminal a.a. will yield ornithine and urea after alkaline hydrolysis. e. The third amino acid gives a positive result for Hopkins-Cole Test. f. Chymotrypsin cannot cleave the peptide bond on the fifth amino acid because of the presence of this a.a. residue. g. The amino acid at the carboxy-end of the third a.a. will yield a black precipitate for Pb(Ac)2.
Define the following terms:a. thiamine pyrophosphateb. lipoic acidc. PHDCd. HETPPe. nucleoside diphosphate kinase
What is the purpose of Southern's blotting technique? Explain in detail the biochemical principle that underpin each step of the method.
Name some techniques/approaches (name, describe the major steps, how to analyze/interpret results) that can be used to satisfy the following requirements: 1. Show that substance is pure protein 2. Only one protein was extracted
(3) What is a protein database? Give examples (and links) of some protein database
A research scholar is interested in separating a protein with 22 kDa. When he performed SDS-PAGE, he obtained a protein band in between 20 and 24 kDa. As SDS-PAGE is not a high-resolution technique; suggest a

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