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- 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 what way can alkaloidal reagents precipitate proteins? In excess of alkaloidal reagent, did the precipitate formed dissolve or not? What is the evidence for your answer?Are Xanthoproteic and Millon Nasse tests satisfactory for use in the urinary examination for protein? Why? 2. Which test can be used to show up to what stage the hydrolysis of a protein proceeds? Why?
- When analyzing urine from a patient with kidney disease, which organicmolecules might be detected? Explain. Which biochemical test will be the most appropriate for detection of those molecules?Describe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.1. As milk ages, bacteria that produce lactic acid increase in number. What will that do to the pH of the milk? 2. when acid was added to milk it got thick and clumped up, Would adding a base have a similar effect? Explain
- Which of the following statements are true about stacking and separating gels? a. The holes is the separating gel are much smaller than the ones in the stacking gel. b. The stacking gel is at a pH of 6.9, while separating gel is at a pH of 8.9 c. The higher pH in separating gel causes the glycine buffer to accelerate more and thus leaving behind the proteins to stack at the interface. d. The smaller holes in separating gel slows down the mobility of the proteins at the interface.What amino acids will be positive at a pH of 2? Use the pKa tableA culture medium contains 1mM NaCl, 1mM of each essential amino acid, and 5g/L honey. Is the medium defined or undefined? How do you know?
- 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?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 precipitateWhat are the following is/are responsible for the denaturation of proteins? Select one: a. All of these b. Organic solvents c. pH change d. Heat