4. Use the cartoon protein below to answer the following questions. Assume the rounder subunits are 45 kDa and the star shaped group is 27 kDa. The lines represent disulfide bonds.
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- Which of the following statements about electron microscopy are true?Group of answer options a.By taking pictures of the same protein frozen in ice thousands of times and then adding them together, you get a high-resolution image of the protein b.Electron microscopy is not used in structural biology as it can not give as high a resolution as X-ray crystallography and NMR c.The smaller a protein, the easier it is to solve its structure with electron microscopy dMost existing protein structures have been resolved using electron microscopy e.The first protein structure with true atomic resolution was solved using electron microscopy last yearWhich of the following statements about electron microscopy are true? a) Most existing protein structures have been resolved using electron microscopy b) Electron microscopy is not used in structural biology as it can not give as high a resolution as X-ray crystallography and NMR c) The smaller a protein, the easier it is to solve its structure with electron microscopy d) By taking pictures of the same protein frozen in ice thousands of times and then adding them together, you get a high-resolution image of the protein e) The first protein structure with true atomic resolution was solved using electron microscopy last year1. outline the principles and procedures of isoelectric focusing. 2. Explain the four levels of protein structure.
- 1. The chromatography solvent is very polar as it contains alcohol, an acid and water. Based on this information, list all the polar amino acids and arrange them from most polar to least polar.SDS-PAGE gels are used to study changes in protein primary structure. Which of the following statements about SDS-PAGE gels is correct? A. The negatively charged proteins will move towards the negatively charged electrode in the SDS-Page chamber B. A detergent is needed to disrupt protein secondary, tertiary, and quaternary structure before a gel can be run C. No "stains" or other treatments are needed to "see" the protein bands on a gel D. Long polypeptides move a further distance from the loading well in a SDS-PAGE gel than short polypeptidesSome characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 75,000 5.0 No 2 12,500 4.8 No 3 73,000 9.8 Yes a. What type of chromatography separates proteins based on their size? b. What type of chromatography separates proteins based on their charge? c. Could gel filtration chromatography be used to separate a mixture containing Protein 2 and 3? Clearly explain why or why not. If gel filtration chromatography can be used to separate Protein 2 from Protein 3, which protein would elute first (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins (Protein 2 and Protein 3) be monitored at 280nm and 400nm (clearly explain)? d. Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by…
- Some characteristics of three proteins are listed in the table below: Protein Molecular Weight (Da) Isoelectric point (pI) Does the Protein Contain a heme moiety? 1 25,000 4.5 Yes 2 77,500 10.8 No 3 75,000 4.9 No a) Could gel filtration chromatography be used to separate a mixture containing Protein 1 and 2? Clearly explain why or why not. If it can be used, which protein would elute last (clearly explain why)? After collecting the fractions from the column, the absorbance of each fraction will be measured using a spectrophotometer. Can both proteins 1 and 2 be monitored at 280nm and 400nm (clearly explain)? b) Which 2 proteins listed in the table above could be separated by ion exchange chromatography but NOT by gel filtration? Why? c) Which 2 proteins listed in the table above could be separated by gel filtration chromatography but NOT by ion exchange chromatography? Why?The elution of a protein with an isoelectric point of 7.5, is mostly likely to be affected by a change in pH from 7.4 to 6.9 in which type of protein separation technique? a.) size exclusion chromatography b.) SDS-acrylamide gel electrophoresis c.) affinity chromatography d.) ion exchange chromatography1. You want to purify a protein using anion exchange column chromatography. In this technique, the solid state beads are positively charged. What charge would you want your protein to have in order for it to "stick" to the beads? Neutral Positive Negative 2. In your anion exchange experiment, your protein of interest has a pI of 6.0. Which of the following buffer solutions would you want to use when loading your protein extract onto the column so that your protein "sticks" to the beads? pH 4.5 pH 7.3 pH 6.0 3. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer consisting of 2 alpha subunits, 1 beta subunit, and 2 gamma subunits, how many bands would you expect to see on your gel? The alpha subunits are 32kDa. The beta subunit is 32kDa. The gamma subunits are 15kDa. 1 5 2 3 4. You want to analyze your chromatography results using gel electrophoresis. If your protein is a pentamer…
- 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.Using the chart below, can you produce a two-step procedure that demonstrates protein purification in protein D from the other proteins? Would you use a size and/or an ion-exchange chromatography? 1. Sketch two chromatograms that demonstrates this behavior.9. Complete the following table by listing our uses of each type of macromolecule.