Which of the following will happen if perchloric acid is added to a neutral polysaccharide gel? (Select 2 Possible Answers) a. increases gel formation b. decreases gel formation c. increases sol formation d. decreases sol formation
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- You are running a size exclusion column to purify your 25 kDa protein from a lysate mixture. The void volume for the column is 10 mL, while the elution volume is 50 mL.The resin is used to separate proteins from 10 kDa up to 100 kDa.After running 75 mL of buffer through the column, you stop and run samples on an SDS-PAGE gel on fractions that showed absorbance values at 280 nm.On your SDS-PAGE gel, none of lanes shows a band at 25 kDa. What is the best possible explanation for the results? y. Your elution buffer did not have a high enough salt concentration to elute your protein. z. Your protein is not globular so runs at a different molecular weight on the SDS-PAGE gel. aa. You did not run enough buffer through the column to elute your protein. bb. Your protein does not absorb at 280 nm due to no solvent exposed aromatic groups.Which of the following options shows the correct order of fastest to slowest motion of chloride ions, glycine and proteins through the separating gel? Chloride ions > Proteins > Glycine Glycine > Chloride ions > Proteins Chloride ions > Glycine > Protein Protein > Chloride ions > GlycineWhat is true about 'cracking' of emulsion? Select one: O a. The primary emulsion does not become white due to coalescence of the dispersed phase O b. The globules of dispersed phase rise to the surface O c. Cracking is reversible and redispersion can be achieved by shaking O d. It is a result of phase inversion due to prolong storage
- There are two proteins in a pH 7 buffer, what you know is: one has a lot of Asp and Glu, the other one has a lot of Lys, Arg and His. Below which approach will get the two proteins separated? gel filtration chromatography ultracentrifugation salting out ion exchange chromatography affinity chromatographyYou have a 20 mg/mL stock solution of the amino acid arginine and need to make plates containing arginine at a concentration of 10 micrograms/mL. How much of the stock solution do you add to 1 liter of plate media?How many grams of sodium chloride is required to render 80ml of 2% solution of ascorbic acid isotonic with blood. using The sodium chloride equivalent of drug = 0.18 Select one: O a. All of the answer is wrong. Ob 0.256 gm O c. 0.576 gm Od 0.432 gm
- Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?Discuss three polysaccharide structural features that promote gel formationUnder what pH conditions can a protein not bind to the beads in a column? pH = -pKa pH = pI pH = 7 pH = pKa In size exclusion/gel filtration chromatography, the elution order is dependent upon Molecular weight Concentration Overall Charge Enzymatic Activity
- Consider a crude extract with a mixture of the 5 proteins listed below. Protein A 4.5 pl 160 molecular weight, kDa Protein B 12.5 pl and 65 molecular weight Protein C 5.0 pl, 15 molecular weight Protein D 6.8 pl, 150 molecular weight Protein E 9.5 pl, 45 molecular weight You load this protein mixture onto an anion exchange column at pH 11. Next, you apply a "washing" step by passing through buffer at pH 11. Finally, for your elution step, you apply a pH gradient starting from pH 11 to pH 2.0 (A gradient buffer system allows you to gradually and continuously change the pH of your mobile phase starting from pH 11 up to pH 2). You load this same protein mixture onto a Size Exclusion column. Please indicate the order in which these proteins will elute for both. Group of answer choices Yes or No, please explain your answer. If your protein of interest is protein A, would using anion exchange column be completely successful at separating it from all the other proteins? Group of answer…Consider a mixture comprised of the proteins below: Protein that will most strongly bind to an anion exchange column is? Protein that will elute first in gel filtration chromatography is? Protein that will elute last in hydrophobic interaction chromatography is? Protein that will elute last in carbohydrate containing column is ?A C2 G This a photograph of an actual polyacrylamide gel that has been run with samples of protein. For each question, write the letter from the item in the gel that best matches the word or concept that is described. Answers may be used once, more than once, or not at all. There may be more than one correct answer per question. 1. Band 2. Lane 3. Well 4. Will protein migrate through the gel from A to B or will it migrate from B to A? 5. Which end is nearest the negative electrode, A or B? 6. Which contains smaller protein fragments, F or G? 7. Which letter indicates the highest concentration of protein fragments that are the same size 8. Where would a sample of protein be loaded? B.