Type I membrane proteins have all of the following properties EXCEPT: cleavable signal sequence N-terminus in...
Type I membrane proteins have all of the following properties EXCEPT:
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cleavable signal sequence |
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N-terminus in the exoplasmic space and C-terminus in the cytosol |
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GPI anchor |
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are transmembrane proteins |
Homework Answers
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Type I membrane proteins have all of the following properties
EXCEPT:
cleavable signal sequence
N-terminus in...
Hydropathy analysis of a membrane protein's amino acid sequence predicts the protein's transmembrane segments and orientation...
Hydropathy analysis of a membrane protein's amino acid sequence predicts the protein's transmembrane segments and orientation in the membrane. It is necessary to confirm those predictions with experimental analysis. One experimental approach for plasma membrane proteins is to use the protease trypsin to digest extracellular domains of these proteins. (Trypsin is hydrophilic and cannot cross the plasma membrane to enter the cell.) When added to cells, trypsin digests the hydrophilic portions of plasma membrane proteins exposed outside the cell into...
hich of the following organelles are the destination for proteins synthetized by cytosolic ribosomes Peroxisomes, endoplasmic...
hich of the following organelles are the destination for proteins synthetized by cytosolic ribosomes Peroxisomes, endoplasmic reticulum, and the Golgi apparatus The Golgi apparatus, lysosomes, and the nucleus Peroxisomes, mitochondria, and lysosomes Peroxisomes, mitochondria, and the nucleus Mitochondria, lysosomes, and the nucleus What is the fate of N-terminus signal peptide after it directs the protein to the ER translocator O It is linked to the transported protein by S-S bond It is cleaved and then released into the membrane It...
Mutation Cremoves the signal sequence from prolon 3 Mutation D prevents the fusion of all vesicles...
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,...
For her research project, Anneka found this great website to predict the transmembrane domains of secretory...
For her research project, Anneka found this great website to predict the transmembrane domains of secretory proteins. An algorithm allows estimating the hydrophobicity of amino acid stretches in the sequence of secretory proteins. Hydrophobic stretches are plotted with positive values on the Y-axis. On the X-axis, Anneka can see the protein sequence expressed as amino acid number, with N-terminus at the intersection with the Y-axis. Example of prediction of TMD domains (a) Human growth hormone receptor (type 1) Nw Signal...
Which of the following is not a function of peripheral proteins? A) mechanical support for membrane...
Which of the following is not a function of peripheral proteins? A) mechanical support for membrane B) enzymes C) receptors D) anchor for integral proteins E) factors that transmit transmembrane signals
Translocation of most proteins into the ER requires all of the following EXCEPT a(n): Select one:...
Translocation of most proteins into the ER requires all of the following EXCEPT a(n): Select one: a. Importin receptor b. Ribosome c. Signal sequence d. Translocon/Sec61 complex e. Signal Recognition Particle
You cut the signal-anchor sequence out of the cDNA for a type II membrane protein and...
You cut the signal-anchor sequence out of the cDNA for a type II membrane protein and express it in cultured human cells and then perform immunofluorescent staining. Describe where this protein should normally be found and where your mutated protein will be found.
Sketch the following proteins, including only the sorting signals, based on their FINAL DESTINATION, listed below:...
Sketch the following proteins, including only the sorting signals, based on their FINAL DESTINATION, listed below: A transmembrane protein (3-span ) in the plasma membrane A soluble protein in the peroxisome (assuming cytosolic route) A soluble ER resident protein A 4-span membrane protein on the Plasma Membrane, with N-terminus in theextracellular space. (Where is C-terminus?) A cytosolic protein A membrane-bound (1-span) ER resident protein A soluble mitochondrial matrix protein
Which of the following statements describing the import of proteins into the nucleus is correct? Answers...
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...
Test yourself Many cell surface trans membrane proteins, called glycoproteins, have an attached c...
Test yourself Many cell surface trans membrane proteins, called glycoproteins, have an attached carbohydrate group, 1. ich faces the extracellular space. This carbohydrate group is attached to the protein when it is still in the rER. Is the carbohydrate attached to the side of the protein that faces the lumen of the rERo the cytosol 2.Explain why the orientation of a transmembrane protein (i.e. which side of the protein faces the inside and which side faces the outside of the...
hich of the following organelles are the destination for proteins synthetized by cytosolic ribosomes Peroxisomes, endoplasmic reticulum, and the Golgi apparatus The Golgi apparatus, lysosomes, and the nucleus Peroxisomes, mitochondria, and lysosomes Peroxisomes, mitochondria, and the nucleus Mitochondria, lysosomes, and the nucleus What is the fate of N-terminus signal peptide after it directs the protein to the ER translocator O It is linked to the transported protein by S-S bond It is cleaved and then released into the membrane It...
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,...
For her research project, Anneka found this great website to predict the transmembrane domains of secretory proteins. An algorithm allows estimating the hydrophobicity of amino acid stretches in the sequence of secretory proteins. Hydrophobic stretches are plotted with positive values on the Y-axis. On the X-axis, Anneka can see the protein sequence expressed as amino acid number, with N-terminus at the intersection with the Y-axis. Example of prediction of TMD domains (a) Human growth hormone receptor (type 1) Nw Signal...
Translocation of most proteins into the ER requires all of the following EXCEPT a(n): Select one: a. Importin receptor b. Ribosome c. Signal sequence d. Translocon/Sec61 complex e. Signal Recognition Particle
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...
Test yourself Many cell surface trans membrane proteins, called glycoproteins, have an attached carbohydrate group, 1. ich faces the extracellular space. This carbohydrate group is attached to the protein when it is still in the rER. Is the carbohydrate attached to the side of the protein that faces the lumen of the rERo the cytosol 2.Explain why the orientation of a transmembrane protein (i.e. which side of the protein faces the inside and which side faces the outside of the...
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