Provide a stepwise, arrow-pushing mechanism for the following transformation. You may use general acid and base as necessary. Feel free to abbreviate structures as needed. Lyase SCOA TPP OH H + H SCOA
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- A vial of Doxorubicin reads 0•5g per vial. Instructions say to reconstitute each 12mg with 2•5ml of NS. How many ml of NS will be needed to reconstitute the vial of the recommended concentration? please show workingExplain why protein purification procedures are normally carried out 4-5°C.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
- 39. The most expensive method to purify the protein is: Affinity Size exclusion RP-HPLC (reversed phase) lone exchangeComplete 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:A cationic microbacteriaI peptide is anaIysed using cation exchange chromatography where the packing materiaI has a negative (-) charge. Choose which buffer system is best used. trishydroxyIammonium ammonia trisaminomethane phosphate
- The 3 proteins have the following properties. Which is the correct order of steps to extract them? + ethyl acetate, + (NH4)2SO4 at 20% saturation, centrifugation, + detergent (Triton X), buffer the lysate (pH=10), centrifugation, collect precipitate + ethyl acetate, + detergent (Triton X), + (NH4)2SO4 at 20% saturation, centrifugation, buffer the lysate (pH=10), centrifugation, collect precipitate + 1 M NaCl, + detergent (sodium dodecyI suIfate), centrifugation, +(NH4)2SO4 at 60% saturation, buffer at pH 7, centrifugation, collect precipitate + ethyl acetate, adjust pH to 7.3, centrifugation, collect supernate, +detergent (Triton X) to precipitate, +(NH4)2SO4 at 30% saturation, centrifugation, collect precipitateSketch the appearance after visualization of a protein mixture containing the seven proteins (fibrinogen, y-globulin, collagen, ovalbumin, myoglobin, hemoglobin, insulin) when subjected to two-dimensional (2D) gel electrophoresis.Identify the most cost effective enzyme purification method and provide brief explanations for this method. ▪Repeated freezing and thawing ▪Sonication ▪Homogenization by high pressure (French press) ▪Homogenization by grinding (bead mill) ▪Permeabilization by detergents (e.g. Triton X-100) and/or enzymes (e.g. lysozyme)
- 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…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 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-Asp