Homework Answers
Answer :-
The SRP which is signal recognization particle recognize an ER signal sequence on N-terminus bind to ribosomal translation complex. Protein is translocated to ER. It's ER signal will be detected as soon as it will emerges from the ribosome . The growing polypeptide chain will be transferred by the ER translocation channel as ribosomes get bound to the ER membrane. Because of the nuclear localization sequence will never be exposed to the cytosol and it will never be recognized and it will never be transported to nuclear pore receptor which will prevent the protein from entering the nucleus.
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27) Consider a protein that contains an ER signal sequence at its...
A protein that has an internal ER-signal sequence and a nuclear localization might end up in...
A protein that has an internal ER-signal sequence and a nuclear localization might end up in the extracellular matrix. in the cytosol. inside a lysosome. o in the plasma membrane.
3. You modify GDP (green fluorescent protein) to contain a signal sequence you believe is a...
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If you deleted the ER N-terminal signal sequence from a gene that encodes a protein, where...
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Please also explain why! Thank you! 18) You want to design an ER transmembrane protein with...
Please also explain why! Thank you!
18) You want to design an ER transmembrane protein with three transmembrane domains with the N-terminal in the ER lumen and the C-terminal in the cytosol. Which of the following arrangement(s) of signals will be required to attain such a topology? A. From N-terminal: signal sequence, start-transfer signal, stop-transfer signal. B. From N-terminal: signal sequence, start-transfer signal, stop-transfer signal, start-transfer signal. C. From N-terminal: signal sequence, stop-transfer signal, start-transfer signal. D. From N-terminal: start-transfer...
3) A protein contains an N-terminal cleavable signal sequence and two further transmembrane domains. How is the protein most likely oriented with respect to the ER membrane? How is it oriented when in...
3) A protein contains an N-terminal cleavable signal sequence and two further transmembrane domains. How is the protein most likely oriented with respect to the ER membrane? How is it oriented when introduced to the plasma membrane after trafficking?
A cell contains a mutant SRP protein that cannot bind the normal signal sequence on target...
A cell contains a mutant SRP protein that cannot bind the normal signal sequence on target proteins. Explain how this would affect the endoplasmic reticulum structure AND function. How would cytoplasmic protein production be affected? Explain your reasoning.
Your lab assistant put together DNA sequences to create a modified polypeptide sequence, then exp...
your lab assistant put together DNA sequences to create a modified polypeptide sequence, then expressed these constructs in some brain cells. For each of the following constructs, predict the intracellular (or extracellular) location, and a brief description of why. Assume a start codon is present. a) a protein normally targetted to the chloroplast stroma, with N-terminal targeting sequence deleted. b) a C-terminal peroxisomal targeting sequence has been asses to the C-terminus of a normally secreted protein, still with its usual...
Please answer all questions 2 After isolating the rough endoplasmic reticulum from the rest of the...
Please answer all questions
2 After isolating the rough endoplasmic reticulum from the rest of the cytoplasm, you purify the RNAS attached to it. Which of the following proteins do you expect the RNA from the rough endoplasmic reticulum to encode? (a) (c) soluble secreted proteins plasma membrane proteins ER membrane proteins all of the above (b) (d) -13 In which cellular location would you expect to find ribosomes translating MRNAS that encode ribosomal proteins? (a) (c) the nucleus in...
In-Class Activity #12, Protein Tratlicking Worksheet 1. You are interested in four different proteins in a...
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Mutation Cremoves the signal sequence from prolon 3 Mutation D prevents the fusion of all vesicles...
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A protein that has an internal ER-signal sequence and a nuclear localization might end up in the extracellular matrix. in the cytosol. inside a lysosome. o in the plasma membrane.
Please also explain why! Thank you!
18) You want to design an ER transmembrane protein with three transmembrane domains with the N-terminal in the ER lumen and the C-terminal in the cytosol. Which of the following arrangement(s) of signals will be required to attain such a topology? A. From N-terminal: signal sequence, start-transfer signal, stop-transfer signal. B. From N-terminal: signal sequence, start-transfer signal, stop-transfer signal, start-transfer signal. C. From N-terminal: signal sequence, stop-transfer signal, start-transfer signal. D. From N-terminal: start-transfer...
Please answer all questions
2 After isolating the rough endoplasmic reticulum from the rest of the cytoplasm, you purify the RNAS attached to it. Which of the following proteins do you expect the RNA from the rough endoplasmic reticulum to encode? (a) (c) soluble secreted proteins plasma membrane proteins ER membrane proteins all of the above (b) (d) -13 In which cellular location would you expect to find ribosomes translating MRNAS that encode ribosomal proteins? (a) (c) the nucleus in...
In-Class Activity #12, Protein Tratlicking Worksheet 1. You are interested in four different proteins in a yeast cell: • protein 1 is a cytosolic protein protein 2 is a secreted protein • protein 3 is a nuclear protein protein 4 is a cell surface membrane protein with N-terminal end in extra-cellular space. a. You plan to study how the proteins are localized to their specific destination by creating the following mutations in the genes encoding proteins 1-4. Indicate how the...
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,...
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