How would you describe the polarity of the enzyme glucose-6-phosphatase, knowing it is a transmembrane protein?
How would you describe the polarity of the enzyme glucose-6-phosphatase, knowing it is a transmembrane protein?
Homework Answers
This enzyme is negatively charged as it contains histidine and arginine which are present to their active site.. This histidine molecule covalently binds to phosphoryl moiety during catalysis. Arginine involves in positioning of phosphate during catalysis.
This will make 9 hellical transmembrane model of this enzyme.
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How would you describe the polarity of the enzyme
glucose-6-phosphatase, knowing it is a transmembrane protein?
Hundreds of mutations in the enzyme glucose-6 phosphatase have been discovered. Why would this impact enzyme...
Hundreds of mutations in the enzyme glucose-6 phosphatase have been discovered. Why would this impact enzyme function?
a) The enzyme glucose 6-phosphatase is essential for the creation of glucose (which passes from the...
a) The enzyme glucose 6-phosphatase is essential for the creation of glucose (which passes from the liver to the blood stream) from pyruvate/glycogen? Choose the right option: pyruvate or glycogen b) Red blood cells lack mitochondria and thus they reduce Pyruvate to Lactate under aerobic/anaerobic conditions. Choose the right option: aerobic or anaerobic c) All enzymes involved in glycolysis are cytosolic. Correct or incorrect? d) The Mg+2 ion is a cofactor of most enzymes that participate in the process of...
explain how you can guess if a specific protein is a transmembrane protein.
explain how you can guess if a specific protein is a transmembrane protein.
5. (9pts) You are studying an ER membrane protein, YFG1 (outlined in yellow), with three transmembrane...
5. (9pts) You are studying an ER membrane protein, YFG1 (outlined in yellow), with three transmembrane domains (rectangles A, B & C at the amino acid positions according to the following map, connected by soluble domains (wavy lines): N-term 10 10 Com Amino acid position (not to scale) 30 60 80 140 160 310 ABCI YFG1 alkaline phosphatase To determine how the protein is arranged in the ER membrane, you construct a series of shortened YFG1 proteins that are connected...
18. How is the activity of glucokinase and glucose-6-phosphatase regulated in liver cells? What is the...
18. How is the activity of glucokinase and glucose-6-phosphatase regulated in liver cells? What is the role of GLUT2 in the hepatocyte membrane?
Protein phosphatases catalyze removal of phosphate groups from proteins. How would the activity of a protein...
Protein phosphatases catalyze removal of phosphate groups from proteins. How would the activity of a protein phosphatase affect a cell's response to growth factors? a) Decrease proliferation b) Decrease glucose production c) Increase proliferation d) Increase glucose production
6a. You have found a new protein of interest: this protein has a transmembrane domain (as...
6a. You have found a new protein of interest: this protein has a transmembrane domain (as predicted by hydropathy analysis). You want to confirm this and determine which portion of the protein is outside the cell and which portion is inside the cell. You begin with a protease protection assay, the results are below. Does this protein most likely have a transmembrane domain? Is the larger portion inside the cell or outside the cell? Is there anything wrong with the...
1. You have identified a new protein and predict it is a transmembrane protein due to...
1. You have identified a new protein and predict it is a transmembrane protein due to its AA sequence analysis. How would determine where the protein is located in the cell? A. Extract all the proteins from the cell and analyze them on a protein gel. B.Use Polymerase Chain Reaction (PCR) to amplify the protein. C. Use an fluorescent antibody to the protein and allow it to bind to the cells. D Isolate the RNA for the protein and use...
9. Draw a hydropathy plot of a 330 amino acid long singlepass transmembrane protein that has...
9. Draw a hydropathy plot of a 330 amino acid long singlepass transmembrane protein that has a TM region beginning at residue 55. Generally, how long would you have to draw the TM region? 17. Describe two examples of membrane protein constraint and why it is important in each system. Draw diagrams.
You are characterizing the binding of a ligand to a protein. Knowing that the rate of...
You are characterizing the binding of a ligand to a protein. Knowing that the rate of association between the protein and ligand is diffusion controlled and that the KD is expected to be around 100 µM, a) What do you expect that half-life of the complex to be? b) What method would you choose to measure the KD? Briefly describe why the method is appropriate
5. (9pts) You are studying an ER membrane protein, YFG1 (outlined in yellow), with three transmembrane domains (rectangles A, B & C at the amino acid positions according to the following map, connected by soluble domains (wavy lines): N-term 10 10 Com Amino acid position (not to scale) 30 60 80 140 160 310 ABCI YFG1 alkaline phosphatase To determine how the protein is arranged in the ER membrane, you construct a series of shortened YFG1 proteins that are connected...
18. How is the activity of glucokinase and glucose-6-phosphatase regulated in liver cells? What is the role of GLUT2 in the hepatocyte membrane?
6a. You have found a new protein of interest: this protein has a transmembrane domain (as predicted by hydropathy analysis). You want to confirm this and determine which portion of the protein is outside the cell and which portion is inside the cell. You begin with a protease protection assay, the results are below. Does this protein most likely have a transmembrane domain? Is the larger portion inside the cell or outside the cell? Is there anything wrong with the...
9. Draw a hydropathy plot of a 330 amino acid long singlepass transmembrane protein that has a TM region beginning at residue 55. Generally, how long would you have to draw the TM region? 17. Describe two examples of membrane protein constraint and why it is important in each system. Draw diagrams.
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