Dowex-50 is a cation exchange resin. Describe the expected elution pattern for mixture of aspartic acid,...
Dowex-50 is a cation exchange resin. Describe the expected elution pattern for mixture of aspartic acid, histidine and arginine amino acid residues that were solubilized in a buffer of pH 7.0. Please explain the answer.
Homework Answers
Dowex 50 being cation exchange resin can trap cations.
It depends on next charge on amino acid.
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Dowex-50 is a cation exchange resin. Describe the expected
elution pattern for mixture of aspartic acid,...
Question 5.A mixture contains Gu, His, Pro, Lys and need to be separated using Dowex 50...
Question 5.A mixture contains Gu, His, Pro, Lys and need to be separated using Dowex 50 cation exchange, prepared in a loading buffer at pH 2.0 : the following buffers are available :- -Amino acid mixture in 0.04 M citrate buffer, at pH 2.0. -0.04 M citrate buffer at 4.5 -0.04 M citrate buffer at 8.0 -0.04 M citrate buffer at 10.5 Assume these amino acids elute only at pH above their perspective pl. Support your answers with clear explanations....
please explain thoroughly and show all work If you applied an amino acid mixture containing Histidine...
please explain thoroughly and show all work
If you applied an amino acid mixture containing Histidine and Lysine onto ion exchange chromatography, at what pH should the chromatography be performed? Explain your reasoning. Lysine: pKa1-2.2, pKa2-9.1 and pKaR- 10.5 Histidine: pKa1=1.8, pKa2-9.3 and pKaR-6.0
If you applied an amino acid mixture containing Histidine and Lysine onto ion exchange chromatography, at what pH should the chromatography be performed? Explain your reasoning. Lysine: pKa1-2.2, pKa2-9.1 and pKaR- 10.5 Histidine: pKa1=1.8, pKa2-9.3 and...
How would you use ion exchange chromatography to seperate a mixture of alanine, glutamic acid, and...
How would you use ion exchange chromatography to seperate a mixture of alanine, glutamic acid, and lysine if you wished to maintain the pH at 7.5 and use only a single ion exchange column ( either an anionic or cationic exchanger). Describe the expected order of elution under the conditions which you propose.
You have a mixture of the proteins listed below. Protein pI Molecular Weight (kDa) A 3.1...
You have a mixture of the proteins listed below. Protein pI Molecular Weight (kDa) A 3.1 265 B 6.9 93 C 10.3 96 D 7.1 43 E 8.6 189 1. You load the protein mix onto a cation exchange column at pH 5. Next, you apply a "washing" step by passing through buffer at pH 5. Finally, for your elution step, you apply a pH gradient starting from pH 2.0 to pH 13.0. (A gradient buffer system allows you to...
c) You place your pentapeptide into a buffer with a pH=4. What direction will your pentapeptide...
c) You place your pentapeptide into a buffer with a pH=4. What direction will your pentapeptide move: Circle the correct answer. (2 marks) It will not move. Towards the positive electrode Towards the negative electrode Briefly Explain why: (2 marks) d) You are trying to separate 2 other peptides from your pentapeptide. Peptide 1 is made up of the amino acids: ARKS Peptide 2 is made up of the amino acids: ADES At what pH would you be able to...
what is the prediction of the unknown amino acids mixture based on the strip from thin layer chromatography sheet? The unknown mixtures can be ala plus asp, ala plus asp plus lys, lys plus asp or ala...
what is the prediction of the unknown amino acids mixture
based on the strip from thin layer chromatography sheet?
The unknown mixtures can be ala plus asp, ala plus asp plus
lys, lys plus asp or ala plus lys.
anion exchange resin was used
Tubes 2,3, 6 and 7 had a spot appear that was light pink
We were unable to transcribe this imageWe were unable to transcribe this imageH-) to the column followed by a sufficient amount of the...
Name Standard Reduction Potentials of Some Biologically Important Half-Reactions TABLE 13-7 Amino...
Name Standard Reduction Potentials of Some Biologically Important Half-Reactions TABLE 13-7 Amino acids pki k2 pkR Half-reaction 2.34 9.60 2.34 9.69 1.99 10.96 2.32 9.62 2.36 9.60 2.36 9.68 Ubiquinone + 2H+ + 2e-→ ubiquinol + H: 0.045 Fumarate:-+ 2H. + 2e-→ succinate"- 2H+ + 2e-→ H2 (at standard conditions, pH 0) 0.000 Crotonyl-CoA+2H +2butyryl-CoA0.015 Oxaloacetate:-+ 2H+ + 2e-→ malate"--0.166 Pyruvate +2H2elactate Acetaldehyde + 2H+ + 2e-→ ethanol FAD +2HFADH2 Glutathione + 2H+ + 2e- Alanine Proline 0.031 228 921...
Part Il Short Amwer Oestions and Problem. There are total of sixty-four 64 10 How does...
Part Il Short Amwer Oestions and Problem. There are total of sixty-four 64 10 How does a protein's amino acid sequence infonce the tertiary structure 5 Points le prints in this section 11. A protein was purified to homogeneity. Determination of the mass by gel-filtration chromatography yields 30 d. Gel-fturation chromatography in the presence of 6 Murea yields a 117.d species and a 22-d species. The same protein was treated with mM B-mercaptoethanol and analyzed using SDS-PAGE. There were hands...
11. From the table in question 10, describe a general technique for separating histidine from a...
11. From the table in question 10, describe a general technique for separating histidine from a mixture of His, Tyr, and Arg using an anion exchange media. At what pH would you equilibrate the column? At what pH would each amino acid elute? charged group 12. Compare the dye-binding protein concentration assays, Bradford and BCA in terms of accuracy and ease-of-use. The dyes bind to different areas of the protein. How does this impact their accuracy? How can you improve...
1.) Describe the goals of a Gel Filtration Chromotography Experiment??? 2.) Explain each key theoretical principle...
1.) Describe the goals of a Gel Filtration Chromotography
Experiment???
2.) Explain each key theoretical principle of a Gel Filtration
Chromotography, and how they help acheive the goal???.
4.) Explain the key equations used in the Gel Filtration
Chromotography experiment and the terms involved in the
equation????
HI im trying to prepare for a lab/report and i have some
questions i could use help with please :) over all having trouble
seeing how everything ties together etc :) thank you...
Question 5.A mixture contains Gu, His, Pro, Lys and need to be separated using Dowex 50 cation exchange, prepared in a loading buffer at pH 2.0 : the following buffers are available :- -Amino acid mixture in 0.04 M citrate buffer, at pH 2.0. -0.04 M citrate buffer at 4.5 -0.04 M citrate buffer at 8.0 -0.04 M citrate buffer at 10.5 Assume these amino acids elute only at pH above their perspective pl. Support your answers with clear explanations....
please explain thoroughly and show all work
If you applied an amino acid mixture containing Histidine and Lysine onto ion exchange chromatography, at what pH should the chromatography be performed? Explain your reasoning. Lysine: pKa1-2.2, pKa2-9.1 and pKaR- 10.5 Histidine: pKa1=1.8, pKa2-9.3 and pKaR-6.0
If you applied an amino acid mixture containing Histidine and Lysine onto ion exchange chromatography, at what pH should the chromatography be performed? Explain your reasoning. Lysine: pKa1-2.2, pKa2-9.1 and pKaR- 10.5 Histidine: pKa1=1.8, pKa2-9.3 and...
c) You place your pentapeptide into a buffer with a pH=4. What direction will your pentapeptide move: Circle the correct answer. (2 marks) It will not move. Towards the positive electrode Towards the negative electrode Briefly Explain why: (2 marks) d) You are trying to separate 2 other peptides from your pentapeptide. Peptide 1 is made up of the amino acids: ARKS Peptide 2 is made up of the amino acids: ADES At what pH would you be able to...
what is the prediction of the unknown amino acids mixture
based on the strip from thin layer chromatography sheet?
The unknown mixtures can be ala plus asp, ala plus asp plus
lys, lys plus asp or ala plus lys.
anion exchange resin was used
Tubes 2,3, 6 and 7 had a spot appear that was light pink
We were unable to transcribe this imageWe were unable to transcribe this imageH-) to the column followed by a sufficient amount of the...
Name Standard Reduction Potentials of Some Biologically Important Half-Reactions TABLE 13-7 Amino acids pki k2 pkR Half-reaction 2.34 9.60 2.34 9.69 1.99 10.96 2.32 9.62 2.36 9.60 2.36 9.68 Ubiquinone + 2H+ + 2e-→ ubiquinol + H: 0.045 Fumarate:-+ 2H. + 2e-→ succinate"- 2H+ + 2e-→ H2 (at standard conditions, pH 0) 0.000 Crotonyl-CoA+2H +2butyryl-CoA0.015 Oxaloacetate:-+ 2H+ + 2e-→ malate"--0.166 Pyruvate +2H2elactate Acetaldehyde + 2H+ + 2e-→ ethanol FAD +2HFADH2 Glutathione + 2H+ + 2e- Alanine Proline 0.031 228 921...
Part Il Short Amwer Oestions and Problem. There are total of sixty-four 64 10 How does a protein's amino acid sequence infonce the tertiary structure 5 Points le prints in this section 11. A protein was purified to homogeneity. Determination of the mass by gel-filtration chromatography yields 30 d. Gel-fturation chromatography in the presence of 6 Murea yields a 117.d species and a 22-d species. The same protein was treated with mM B-mercaptoethanol and analyzed using SDS-PAGE. There were hands...
11. From the table in question 10, describe a general technique for separating histidine from a mixture of His, Tyr, and Arg using an anion exchange media. At what pH would you equilibrate the column? At what pH would each amino acid elute? charged group 12. Compare the dye-binding protein concentration assays, Bradford and BCA in terms of accuracy and ease-of-use. The dyes bind to different areas of the protein. How does this impact their accuracy? How can you improve...
1.) Describe the goals of a Gel Filtration Chromotography
Experiment???
2.) Explain each key theoretical principle of a Gel Filtration
Chromotography, and how they help acheive the goal???.
4.) Explain the key equations used in the Gel Filtration
Chromotography experiment and the terms involved in the
equation????
HI im trying to prepare for a lab/report and i have some
questions i could use help with please :) over all having trouble
seeing how everything ties together etc :) thank you...
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