Please provide a chromatography technique to isolate the protein A from the mixture containing protein A and B (shown as below). And explain the separation mechanism related to this example. Protein A: MKRHRRKKHHRKRRKKRKGH (positively charged) Protein B: MDEEEEDDDEEDDEEDEDEED (negatively charged)
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- Please provide a separation solution of combining two types of chromatography to isolate the protein A from the mixture containing protein A, B, C and D (shown as below). And then explain the related mechanisms in details. Protein A: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu- Protein B: Met-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu Protein C: Met-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val- Ile-lle-lle-Leu-Leu- Leu-Leu-Val-Val-Val-lle-lle-lle-Leu-Leu-Leu-Leu-Val-Val-Val-lle-lle- lle-Leu-Leu-Leu-Leu-Val-Val-Val-Ile- Protein D: Met-Asp-Glu--Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Asp- Glu-Asp-Glu-Glu-Asp-Asp-Glu-Glu-Glu-Glu-Asp-Asp-Asp-Glu-Glu-Asp-Asp-Glu-Glu- Asp-Glu-Asp-Glu-Glu-Asp-Glu-Glu-AspAn allosteric enzyme is purified and determination of its mass by gel-filtration chromatography yields 240 kDa. Chromatography in the presence of 6M urea yields a 30 kDa species and 90 kDa species. SDS-PAGE in the presence of Beta mercaptoethanol reveals 2 protein bands of 30 kDa and 45kDa. Describe the quatranary structure.A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol, three bands are again formed, this time with molecular masses of 160, 90, and 60 kDa. Determine the subunit composition of the protein and clearly explain how you came to this determination.
- Complete the table below by adding (+) or (-) if eahc sample (amino acid or protein) below will test positive or negative, respectively. sample BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOSKIN-COLE G W H Y C R HAIR GELATIN CASEIN PEPTONE Identify the amino acid that will give the following data: BIURET NINHYDRIN XANTHOPROTEIC MILLON-NASSE SAKAGUCHI LEAD ACETATE PAULY HOPSKIN-COLE - + + + - - + - Name of amino acid: structurte of the amino acid: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.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? Explain
- Explain in details how you could separate a mixture of three amino acids Arg, Lys, and Cys using ion-exchange chromatography. For the toolbar, press ALT F10 (PC) or ALT+FN+F10 (Mac). ...Given the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3.A solution contains a mixture of four proteins: urease, ovalbumin, lysozyme, and alkaline phosphatase. The proteins have the following properties. Molecular weight (Daltons) Protein pl Urease 483,000 5.0 Ovalbumin 45,000 4.6 Lysozyme 86,000 11.0 Alkaline 86,000 4.6 Phosphatase Based on the information provided, what type of chromatography (gel permeation or ion exchange) could be used to separate: a) Lysozyme from Alkaline Phosphatase. Briefly explain your answer. b) Ovalbumin from Alkaline Phosphatase. Briefly explain your answer. c) Which of the four proteins would be bound to a cation exchanger equilibrated at pH 5? d) Briefly explain your answer to part c).
- A purified protein fraction has a total sample volume of 450 µL. The sample has a corrected A280 of 0.244, and the blank corrected A280 was 0.077. (Both values were measured with a path length of 1.00 cm.) If 5.50 µL of the sample was used in a reaction, calculate the mass of protein in the reaction (in µg).Given the Ramachandran Plot below, identify the protein components that could adopt the phi-psi angle combination indicated by the number 3. (IF YOU COPY UR ANSWER FROM ANOTHER WEBSITE I WILL DISLIKE)Give other chromatographic techniques that can be used for separating non-polar biomolecules, such as lipids. Explain the principle in terms of lipid separation.