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![The proteins given below are separated using CM cellulose at pH 7.0
Write the order of elution of these proteins from the column
Proteins
pl
Fibrinogen
5.8
Hemoglobin
7.1
Lysozyme
11.0
Pepsin
1.0
Ribonuclease
7.8](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F37c2cb94-16db-49cd-b4ed-7dec22749899%2F2f55513e-ccab-4781-aff9-9b03a24c3da3%2F4cuivs_processed.jpeg&w=3840&q=75)
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- Use the following information to answer the following questions."The native structure of hemoglobin (HB) comprises of two α and two β subunits, each of which carries a heme group. There appear to be no previous studies that report the in-vitro folding and assembly of Hb from highly unfolded α and β globin in a 'one-pot' reaction. One difficulty that has to be overcome for studies of this kind is the tendency of Hb to aggregate during refolding. This work demonstrates that denaturation of Hb in 40% acetonitrile at pH 10.0 is reversible." (J Am Soc Mass Spectrum 2007, 18, 8-16)Which of the following statements about hemoglobin is most consistent with the information in the passage? Group of answer choices A. a tertiary protein with two polypeptides B. a quaternary protein with two polypeptides C. a tertiary protein with four polypeptides D. a quaternary protein with four polypeptides When nucleotides polymerize to form a nucleic acid, ________. Group of answer choices A. a…After staining an SDS-PAGE gel with Coomassie Blue G-250, the protein bands are visualized by de-staining the gel in a Coomassie Blue G-250 de-staining solution. This solution is made up of 10% acetic acid, 50% methanol, and 40% distilled water. How much of each of these components do you need to prepare 5 liters of Coomassie Blue G-250 de-staining solution?Given the following information, which protein would be most difficult to isolate from protein X through salting out and dialysis? Protein X: pl = 2.8, MW = 621.51g/mol, Sequence: EDDDE Protein A: pl = 6.0, MW = 658.67g/mol, Sequence: GGAAGGGAAA Protein B: pl = 3.1, MW = 580.55g/mol, Sequence: DSWSS Protein C: pl = 12.5, MW = 586.74g/mol, Sequence: KRKR O A. Protein A O B. Protein B C. Protein C O D. Proteins A, B, and C can be isolated from Protein X through salting out and dialysis
- Electrophoresis is performed at PH 6.8 on a mixture of mutated hemoglobin that differ from normal haemoglobin (Hb) only by the substitution of one amino acid- Hb X: Val replaced par Glu - Hb Y: Asp replaced by Leu - Hb Z: Glu replaced by Lys What will be the order of migration between cathode and anode of these mutated Hb compared to normal Hb? Justify your answer.a. An oligopeptide ALVGALGATPTPQMWSHSWRGVSIKS was digested with trypsin.Which method would be most appropriate for separating the products: ion exchange or gel filtration chromatography? Explain.b. Suppose that the peptide was digested with cyanogen bromide. What would be the optimal separation technique? ExplainBovine chymotrypsin is a serine protease. The enzyme is structurally stable over the pH range of 4.0 – 10.0. It exhibits optimum protease activity in the pH range of 7.5 – 9.0, but its protease activity is strongly inhibited at pH < 6.0. Based on your knowledge of serine protease mechanisms, how would you explain this effect of pH on chymotrypsin’s mechanism of catalysis?
- In a mixture of five proteins listed, draw an elution profile (Absorbance vs. mL eluted, arbitrary) for the purification of the listed proteins on a gel filtration chromatography resin: cytochrome c (pI = 5.4; Mr = 13,000), immunoglobulin G (pI = 7.3; Mr = 145,000), ribonuclease A (pI = 9.6; Mr = 13,700), RNA polymerase (pI = 6.3; Mr = 450,000), human serum albumin (pI = 5.4; Mr = 68,500). Label your elution peaks. Draw a sketch of an SDS-PAGE, reflecting the mobility of the above mixture as they elute from the column. Label you protein bands.Please note when values are sourced from an appendix/table. Include any assumptions.Also please explain why you chose the column based on the column and the protein properties
- H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14The following proteins were separated by SDS-PAGE in the presence of mercaptoethanol. Sketch the relative positions of the various polypeptides on the gel. Label the positive and negative ends of the gel.Protein A: 40 kDa single polypeptideProtein B: 80 kDa protein, made up of two subunits of molecular weight 20 kDa and 60 kDa, held together by noncovalent interactionsProtein C: 200 kDa protein, made up of four identical subunits (50 kDa each) linked together by disulfide bondsA mixture of Asparagine (pl 5.41), Aspartic Acid (pl 2.98), Histidine (pl 7.59), Lysine (pl 9.74) and Threonine (pl 6.53) are separated by cation exchange chromatography. What is the order of elution of these amino acids if you use gradient buffer system from pH 10 to pH 2: v First 1. Asparagine v Second 2. Aspartic Acid 3. Histidine v Third 4. Lysine v Fourth 5. Threonine v Fifth 6. No separation