(b) Why does solution pH affect separation of proteins via electrophoresis? (c) With reference to a labelled diagram, what is the principle of separation via capillary zone electrophoresis (CZE)?
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- Of the components in the hydrogels beads, which is the protein we are interested in measuring?a. Why proteins are extracted to a buffered solution? Briefly describe the components of ageneralized protein extraction buffer?.b. Describe the basis of affinity chromatography in protein purification.c. What is the most appropriate method of protein elution in affinity chromatography?d. List three examples of commonly employed combinations of ligand and protein in affinitychromatography.Is an SDS-PAGE gel, what characteristic is used to separate the proteins? Which proteins move quickly? Which ones move slowly?
- If you added three proteins (Protein A, pI 5.0; Protein B, pI 6.0; Protein C, pI 7.0) to an anion exchange column equilibrated with bicine buffer, pH 8.5, in what order would these protein be expected to elute as the column was loaded, washed, and then increasing amounts of NaCl were added?(a) The octapeptide AVGWRVKS was digested with the enzyme trypsin . Which method would be most appropriate for separating the products: ion-exchange or gelfiltration chromatography? Explain. (b) Suppose that the peptide was digested with chymotrypsin . What would be the optimal separation technique? Explain.If a pediatric vitamin contains 1500 units of vitamin A per milliliter of solution, how many units of vitamin A would be administered to a child given 2 drops of a solution from a drpper calibrated to deliver 20 drops per milliar of solution?
- Using ultrafiltration, you concentrate a solution of Protein X as follows: Initial volume protein X = 300 mL Initial concentration protein X = 12 mg/mL Final volume protein X = 15 mL What's the final concentration of protein X in mg/mL?Sketch 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.What is the diference between soluble and insoluble iber?
- How can contaminants in DNA and RNA samples affect absorbance at 260 and concentration results?Total protein: Do you think that refractive index could be used as a regular method for serum protein determinations? If yes, what limitations does it have. If not, why not? What are the major interferences in the biuret method? Refractometry method?Consider the following properties of the protein components of a sample mixture as provided in the table below: 1. if the mixture is subjected to gel filtration chromotography which protein component elute first? 2. if the mixture is subjected to isoelectric focusing which protein will stop m oving nearest to the positive electrode? 3. if the mixture is subjected to cation-exchange chromotography using a buffer at ph 7 which protein will bind to the resin? 4.if the mixture is subjected to SDS-PAGE which protein will be at bottomost portion of gel? 5.if the mixture is subjected to hydrophobic interaction chromotography which protein will bind most strongly to the resin?