A Transmembrane Protein in The Vesicle
Homework # 2 1. Based on the indicated signal sequence, match where the protein ultimately ends up. Not all answers will be used. Some answers may be used more than once. (4 points, 1 point each) I. __________ An ER signal sequence, a stop transfer sequence, A. Nucleus and a KDEL sequence B. ER lumen II. __________ An ER signal sequence C. Lysosome D. Plasma membrane III. __________ An ER signal sequence and Mannose 6 phosphate E. ER membrane F. Mitochondrial membrane IV. __________ An NLS at the C terminus and an ER signal sequence at the N-terminus G. Secreted from the cell H. Cytoplasm 2. You have the following vesicle below with a transmembrane protein in the vesicle. The vesicle is in the cytoplasm of the cell. 6 points A. Label the cytosolic and non-cytosolic sides of the vesicle. B. Indicate on the protein above where the ER signal sequence was before it was cleaved off by signal peptidase while in the ER. C. Draw the vesicle after it has fused with the plasma membrane. Make sure to indicate the two different sides of the lipid bilayer (___ versus – – – ), the cytosolic and extracellular space, as well as labeling the N and C terminus of the protein 2. You have created a GFP fusion to a protein that is normally secreted from yeast cells. You obtain three mutant yeast strains, each defective in some aspect of the protein secretory process. You also obtain a wild-type control strain. You decide to examine the fate of your GFP fusion protein in these various yeast strains and engineer the mutant strains to express your GFP fusion protein. However, in your excitement to do the experiment, you realize that you did not label any of the mutant yeast strains and no longer know which strain is defective in what process. You end up numbering your strains with the letters A – D, and then you carry out the experiment anyway, obtaining the results shown below (the black dots represent your GFP fusion protein). Write in the number(s) of the indicated proteins that if they were defective would result in the above phenotype for each strain. Remember, one of these is the wild type (normal) strain. Not all answers will be used, some may be used more than once. (8 points, 2 points each) Strain A: _________________________________________ 1. Clatherin Strain B: _________________________________________ 2. Arf and Sar Strain C: _________________________________________ 3. Rab GTPase (specific to its target membrane) Strain D: _________________________________________ 4. Ran GTPase (specific to its target membrane) 5. Nothing 6. COPI 7. COPII 8. SRP 4. You are developing an artificial electron transport chain. Your activated carrier molecule A has a redox potential of 320 mV. And you have two molecules that you think could be downstream of your activated carrier molecule, B with a redox potential of -450 mV, and C with a redox potential of + 30 mV. (3 points; 1.5 points each) A) Which molecule will your activated carrier molecule donate its electrons to? B) Would your molecule in question 4A be in the oxidized or reduced state before the electrons were donated? Extra credit (3 points; 0.5 points each) A. What ribosome is the tethering protein made on? B. What ribosome is clatherin made on? C. How would you be able to determine which ribosomes ATP synthase was made on? D. Where is the ATP made in a cell? (Specify location within organelle). E. What ribosome is AP2 made on? F. What ribosome is a protein in regulated secretion made on?
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