What would happen in each of the following cases? Assume in each case that the protein involved is a soluble protein, not a membrane protein.
Answer:
A):
B):
C):.
D):
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What would happen in each of the following cases? Assume in each case that the protein...
According to these results plasma membrane protein B primary structure will include the following features mRNA B Reticulocytes+++ S35Met Proteases Microsomes Tunicamycin Radioactivity captured in a film Two regions of around 20 hydrophobic amino acids long, at least one Asn in the consensus sequence Asn-X Ser/Thr in between the two hydrophobic areas and a sorting signal for the plasma membrane Two regions of around 20 hydrophobic amino acids long and at least one Asn in the consensus sequence Asn X-Ser/Thr...
Which of the following statements describing the import of proteins into the nucleus is correct? Answers A-D A Transport into the nucleus requires the activity of a G protein. B The receptor for nuclear proteins is found in the cytosol and travels into the nucleus with the protein being transported o С Proteins destined for the nucleus are transported in a fully-folded conformation. D These statements are all correct. o You are interested in a water-soluble protein that functions within...
If the pinsulin receptor, a, example of an integral membrane protein, is cotranslationally inserted into the ER membrane with the N-terminus on the cytosolic side of the membrane and the C-terminus in the lumen of the ER, which side of the protein would you expect to bind to the ligand, pinsulin, when the protein is found on the cell surface? A. N-terminal end of the protein will bind pinsulin B. Neither will bind to a ligand because both ends of...
Mutation Cremoves the signal sequence from prolon 3 Mutation D prevents the fusion of all vesicles to the cell membrane 2. You are studying a transmembrane cell surface protein called Hip in yeast cells. You generate a wild-type Hip-GFP fusion protein and 2 mutant proteins as shown below: M Wild-type protein-GFP Hip GFP Stretch of 6 hydrophobic amino acids Stretch of 18 hydrophobic amino GFP Mutant 1-GFP N- Mutant 2-GFP N- You examine yeast cells expressing the above proteins separately,...
3. You modify GDP (green fluorescent protein) to contain a signal sequence you believe is a novel ER import signal at the N-terminus and a stop transfer sequence 43 amino acids from the N terminal import signal. When this protein is expressed in cells, you see 70% GFP in the cytoplasm and the remainder in the ER. You assume GFP import is occurring. However you cannot rule out some GFP might not fold properly even though it is fluorescent, perhaps...
What would you expect to happen to a newly synthesized soluble protein if a mutation caused the deletion of the KDEL sequence? a. The protein would be returned to the ER in COPI-coated vesicles. b. The protein will be carried forward through the Golgi apparatus. c. The protein will be trapped in COPII vesicles . d. The protein will be incorporated into COPI vesicles. e. The protein will be recognized by KDEL receptors and a retrieval sequence (KDEL sequence) will...
If you deleted the ER N-terminal signal sequence from a gene that encodes a protein, where would the protein end up after synthesis? (Assume no other signal sequences are present) The golgi The smooth ER The protein would be secreted from the cell The cytosol The lysosome
21: Met c aion of the Polamino 21. Which of the following would NOT Change the structure and function of a protein A Methylation of a protein B. Lipid modification of a protein C. Change in the length of the Poly A tail of the mRNA transcript encoding a protein D. Change in the position of reactive amino acids E. Proteolysis 22. Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino acids...
please answer all that you can 1. You have genetically engineered green fluorescent protein (GFP) containing a KDEL sequence (GFP-KDEL). When GFP-KDEL is expressed in normal human fibroblasts and examined using fluorescence microscopy, the fluorescence appears diffuse across the cytoplasm. How would you explain this observations given that KDEL is supposed to be an ER-specific sorting sequence? A. This engineered GFP would not have a hydrophobic signal sequence to get it into the RER in the first place. B. The...
b and d please. c is an example
3. (25 points) You have predicted the amino acid sequences of several proteins based on their open reading frames. The significant domains are shown below. Diagram the final localization(s) (only as far as the ER or nucleus) and any orientation of domains for each protein. Also, indicate all regions that could be GLYCOSYLATED for each protein. No explanation needed if diagrammed and labeled clearly. Empty rectangle = 25 amino acid hydrophobic-rich sequence...