Q: 9. The water-soluble vitamins B₁ (thiamine hydrochloride), B₂ (riboflavin), B3 (niacinamide), and B…
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A: It is to explain that whether the number of spots shown on SDS-PAGE electrophoresis is dependent on…
Q: Show calculations for making 1X TAE gel running buffer and 1.25% agarose gel for your experiment.
A: Buffer is a solution that tends to maintain pH of the solution when acid or base is added to it.…
Q: The first step in the procedure asks you to prepare five dilutions of the protein standard (BSA) in…
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Q: How is matrix selected in soft ionization? Give three examples.
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A: Since you have posted a question with multiple sub-parts, we will solve first three subparts for…
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A: To tell the color of precipitate formed of anilide of acetyl chloride and acetic anhydride.
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Q: Explain the order of elution (with a buffer of pH 4) of the following pairs of amino acids through a…
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Q: At pH 5.0? Q2) (a) Draw the structure of the predominant form (principal species) of…
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Q: Write with the reasons why a separation will occur when a mixture of polypeptides with isoelectric…
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Q: The pNa of a mixture prepared by mixing 200 ml of 0.00063 M of Nacl and 300 ml of 0.00040 M in…
A: The value of pNa is calculated by finding the concentration of Na+ ion in the mixture.
Q: What would be a suitable blank for an assay where the samples contain protein in a solution with dye…
A: A question based on absorption that is to be accomplished.
Q: Use the following chromatogram of standard amino acids: 24 16 19 21 12 15 6,6 9 10 23 13 14 17 18 10…
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Q: The electrophoresis of a sample containing 2-amino-4-methylpentanoic acid. (pKa of a-COOH = 2.2, pKa…
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Q: In what order would histidine, serine, aspartate, and valine be eluted with a buffer of pH 4 from a…
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Q: Indicate the effect (increases, decreases, or stays the same) that each of the following changes…
A: A question based on analytical separations that is to be accomplished.
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A: b) A resin with sulfonic acid group is the correct option.
Q: Draw a titration curve for the tetrapeptide Trp-Asp-Lys-Gly. Label all pK,s, the pl and the net…
A: Trp-Asp-Lys-Gly
Q: Discuss the principles of the colorimetric and enzymatic methods for quantitating uric acid.
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Q: Describe the difference between an oil-in-water and a water-in-oil emulsion, and explain the use of…
A: An emulsion is formed by combining two liquids which don't mix in to each other.
Q: What are the chief differences between the Ninhydrin and Bradford assays for amino acid…
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Q: Which of the following is not a component of the mobile phase in Ion exchange chromatography
A: Phase of mobility (Eluent)- Eluents for ion exchange chromatography are typically made up of an…
Q: Based on the graph, the retention of 4-aminobenzoic acid is not affected changes in mobile phase pH…
A: 4-amino benzoic acid remains in zwitterionic form in ph range 2-9 (approx) so on changing ph of…
Q: which of the following chromatographic methods is best used for separating amino acids?
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Q: Plot the titration curves of valine and lysine amino acids in basic medium and calculate the pI…
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Q: 3. Isoelectric focusing is a separation technique that takes advantage of the differences in…
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Q: If prior to the analysis, the protein X needs to be solubilised in 250 mM acetate buffer, pH 4.0 to…
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Q: When analyzing a PTH (phenylthiohydratoin) derivative of the amino acid isoleucine, resulting from…
A: Reversed-Phase Chromatography: It is a liquid chromatography technique that involves the separation…
Q: titrimetric profile of lysine
A: Rough diagram
Q: what is The method that would be BEST to use to monitor protein secondary structure during the…
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Q: Write one similarity between physisorption and chemisorption.
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Q: 8. What properties cause the separation of amino acids in paper chromatography?
A: Different amino acids have different partition coefficient between water and organic solvent.…
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A: We have to find out the direction of movement of peptide at pH=1.54
What are the basic medium, acid medium, and zwitterion formulas of phenylalanine?
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- The pka of ascorbic acid is 4.2 at 24C. At what pH is the ratio of the deprotonated form to the protonated form 10:1? Prove using the Henderson-Hasselback equation. How to resolve this.. For valine, methionine, GABA and proline, write the zwitterion. Using valine as an example, describe the behavior of the zwitterion in acidic (pH 2) and alkaline (pH 12) media.Based on the graph, the retention of 4-aminobenzoic acid is not affected changes in mobile phase pH because it is zwitterionic. True of Flase?
- Given pKa values for ionizable groups from Table 27.2, sketch curves for the titration of Q.) histidine with NaOH.Draw a diagram (picture) showing the principle species in solution as a function of pH for a mixture of 0.0200 M formic acid and 0.0100 M ascorbic acid. The Y axis should be concentration. The X axis should be pH and you will need to look up the pKa valuesDoes the titrated amino acids appear to be acidic, basic, or neutral amino acids? Please explain your conclusion with reference to the data and to theory.
- If the pH of a solution of Arginine is equal to a half of the 3 pka values of all of its functional groups, what will be the charge on the majority of the Arg molecules in that solution? Please explain. Am i supposedd to add up the three pka values and then divide it in half to find the pH? ThanksDescribe how to prepare a 2.5% 48 ml agarose gel with 1X TBE buffer.You are supplied with the following: NaCl (Mr = 58.443 g/mol) 2.5 M Tris-Cl, pH 8 oplossing / solution (1 Litre) EDTA, sodium salt (Mr = 380.2 g/mol) 10 % Sodium dodecyl sulfate solution Proteinase K solution (50 mg dissolved in 1 ml ddH2O) You need a digestion buffer consisting of the following: 15 mM NaCl 75 mM Tris-Cl, pH 8 16 mM EDTA, pH 8 0.8 % Sodium dodecyl sulfate 0.75 mg/ml proteinase K Calculate: How will you prepare 500 ml of the digestion buffer? Show all your steps and calculations and remember to explain how exactly you will make it up.
