Question 1: Which separation technique exploits the solubility differences of proteins?
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- Figure 3: ● ● ● ● ● ● KDa ● 97.4 66.2 45.0 ● 31.0- 21.5 14.4 S-1 p-1 S-2 2-0 This figure was generated by centrifuging a pura sample of protein, removing the supernatant, and resuspending the pellet in the same volume as the supernatant to allow direct comparison. The supernatant and pellet samples were then prepared for SDS-PAGE identically and run via normal SDS-PAGE procedures. In the figure, "s" means supernatant and "p" means pellet. The text or number after the dash represents a different condition. For example, s-1 and p-1 are the supernatant and pellet samples under condition 1. It is not shown, but under wild-type conditions, essentially all of the protein is found in the supernatant. S-3 ● What does the intensity of each band represent? ● Would you find soluble protein in the supernatant or pellet? Why? Would you find aggregated protein in the supernatant or pellet? Why? For each condition (there are 5 different conditions), is there a higher percentage of the total protein…What features of protein structure allow separation by Size exclusion ("gel-filtration") chromatography: (explain your answer)Answer the following questions. 1. What is Amino Acid and its relation to proteins? 2. What is the importance of using multiple purification methods in isolating a protein?
- Answer choices : 0.3% gel OR 1.0% gel Explanation Choices : Agarose makes smaller pore sizes which leads to sharper distinction of larger bands OR Agarose makes larger pore sizes that enable better separation of larger bands.I wany handwritten solution with full explanation....asap...i will upvoteA mixture of proteins contains Pepsinogen (35 kDa), Fumarase (49 kDa), Transferrin (80 kDa) and Thyroglobulin (340 kDa). Rank these proteins based on the order of their elution from a gel filtration column (1 being the first one to elute and 4 as the last one). Throglobulin Pepsinogen Fumarase Transferrin
- Question 28 : In a SDS-PAGE analysis (Indicate the right answer) : A- The proteins are denatured and positively charged by the addition of SDS. B- Large proteins run faster than small proteins. C- If the pHi of a protein corresponds to the pH of the running buffer the protein becomes positively charged (+) and cannot migrate anymore into the gel. D- For reducing disulfide bridges one needs to add a reducing agent such as 2-mercaptoethanol or DTT. E- All is wrong.Name one purification method that can separate Protein A from a solution that contains all four proteins. (Size exclusion chromatography, ion exchange chromatography, Purification by affinity chromatography, High pressure liquid chromatography, Isoelectric focusing, SDS-PAGE, or Two-dimensional Electrophoresis) 2. In picture 3. In picture 4. In picture 5. In picturePlease 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)
- QUESTION 1: What is the purpose of adding sodium hydroxide (NaOH) to the cheek cell pellet, after removing Phosphate Buffered saline, on p. 55 of the extraction protocol? Note: You might need to conduct an internet search to answer this question. The answer must be in your own words.A 49-year-old man with myeloma was referred for management by the clinical haema- tology team who requested and observed the following biochemistry results analysed on the main automated biochemistry analyser (reference ranges are given in brackets): Sodium Potassium Urea Creatinine Alkaline phosphatase Alanine aminotransferase Albumin Total protein Bilirubin Calcium 131 mmol/L 3.6 mmol/L 5.6 mmol/L 124 μµmol/L 135 IU/L 42 IU/L 30 g/L 140 g/L 15 μmol/L 3.02 mmol/L (135-145) (3.5-5.0) (3.5-6.6) (70-150) (95-320) (5-42) (35-50) (60-80) (<17) (2.12-2.62) (a) What is the electrolyte abnormality in this patient? (b) The sample was subsequently analysed on a direct reading ion-selective electrode for sodium and a result of 144 mmol/L was produced. Explain the difference between the sodium results obtained and state which is the more clinically relevant result.Topic: Determination of Protein Concentration by Spectrophotometry: The Standard Curve The use of Beer-Lambert’s law to estimate the concentration of protein samples is limited only to dilute solutions. Explain why