The following peptides were separated using ion-exchange chromatography based on the use of an anion exchange resin. Which peptide was eluted first? Peptide Name A B C D Molecular Weight (g/mol) 360 1080 1800 1440 Peptide Net Charge -2 0 +1
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- Which method of chromatography would be the most appropriate for separating mixtures of thefollowing peptides at a neutral pH? (a) ARDDEKLLML, LMYWWILLDETSARALIV, DQNNA(b) GATSKKIVLM, ASCILLVMEN, MFDDAAYVNE(c) KLMDAATSPFLMAGHHHHHH, MFPSATEKRQQNNESTVLAG In what order would the following peptides be eluted from an anion exchange column at pH 7.5?Peptide 1: Ala–Asp–Glu–Gln–Trp–Leu–His–ValPeptide 3: Phe–Gln–Glu–Ala–Gln–His–Leu–Arg-IlePeptide 2: Arg–Ile–Pro–Lys–Cys–Met–LysPlease draw the given peptide and calculate the net charge at pH 1, 4, 8 and 12. GRNVGHEWAA biochemist wants to separate two peptides by ion-exchange chromatography. At the pH of the mobile phase to be used on the column,one peptide (A) has a net charge of −3 due to the presence of more Glu andAsp residues than Arg, Lys, and His residues. Peptide B has a net charge of+1. Which peptide would elute first from a cation-exchange resin? Whichwould elute first from an anion-exchange resin?
- Please calculate and plot the charge on a peptide with the sequence of NEYK over the pH range from 1 to 13. Please use the pKa values from the table. You may calculate the charge at 1 pH unit intervals.Draw the peptide PVLED and determine the following: Isoelectric point, pI The net charge at pH = 3.2 ; pH = 7.6 and pH = 9.3 Complete name of the peptide Name using the 3-letter codeUsing mass spec, the primary structure of 4 peptides is obtained from a tissue sample: VMDEL, GHKRT, CNPQI, and SAWFY. The pI of each peptide is calculated and ion exchange chromatography is used to purify each peptide. VMDEL, GHKRT, CNPQI, and SAWFY were separated into 4 pure samples. The labels on all the samples are erased by mistake, and the mass spec is no longer working. You can run a few simple tests to identify the samples. What are 4 tests to identify each peptide and why?
- Above or below what pH would the polypeptide become fully mobile on a cation exchange column? Explain reasoning please. Per my understanding, I believe I need to find pI and then select a pHExamine the following peptide and the inserted table, and answer the 2 questions below: Thr-Glu-Pro-Ile-Val-Ala-Pro-Met-Glu-Tyr-Gly-Lys 1. Estimate the net charge of the peptide at pH 2.0. Explain. 2. Estimate the net charge of the peptide at pH 7.0. Explain.Before high performance liquid chromatography (HPLC) methods were devised for the separation and analysis of small peptides, electrophoresis on a paper support was frequently used. Separation was affected on the basis of the charge on a peptide at different pH values. a. Calculate the pI (isoelectric point) of the following primary structures of the following protein i.) Lys- Gly- Ala- Glyii.) Lys- Gly-Ala-Gluiii.) His- Gly- Ala- Gluiv.) Glu- Gly- Ala -Gluv.) Gln-Gly-Ala-Lys b.) the migration toward the cathode, the negative pole; A for the migration toward the anode, the positive pole; and O if the peptide remains stationary.
- Five amino acids were subjected to normal phase chromatography, and the following Rf values were computed: A - 0.59 B - 0.12 C - 0.71 D - 0.33 E - 0.20 Which is the most polar amino acid?An amino acid mixture consisting of lysine,leucine, and glutamic acid is to be separated by ion-exchangechromatography, using a cation-exchange resin at pH 3.5, with theeluting buffer at the same pH. Which of these amino acids will beeluted from the column first? Will any other treatment be neededto elute one of these amino acids from the column?When performing a separation by ion-exchange chromatography, the rate of elution of an amino acid is influenced by three main factors: a. Temperature b. Solution (buffer) pH c. Ionic strength (buffer concentration) of the eluent Briefly, explain how each of these parameters influences elution rate. Please provide only typed answer solution no handwritten solution needed allowed