You discovered a protein that binds GTP-bound, but not GDP-bound tubulin. Where on a polymerized microtubule...
You discovered a protein that binds GTP-bound, but not GDP-bound tubulin. Where on a polymerized microtubule would you likely find it? Explain your answer.
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You discovered a protein that binds GTP-bound, but not GDP-bound
tubulin. Where on a polymerized microtubule...
How does a GTP cap prevent a microtubule from falling apart, and how does a microtubule...
How does a GTP cap prevent a microtubule from falling apart, and how does a microtubule lose its GTP cap? If the rate of adding GTP-heterodimers to a microtubule is greater than the rate of GTP hydrolysis, then will the microtubule continue growing or fall apart? Explain your answere. Assume that in a normal cell the average length of microtubule reaches before falling apart is 8 micrometers. Imagine a cell with mutant B-tubulin that catalyzes hydrolysis at a rate slower...
Protein purification. The protein tubulin assembles into microtubule fibers and is a major structural component of...
Protein purification. The protein tubulin assembles into microtubule fibers and is a major structural component of your neurons. Microtubule-associated proteins (“MAPs”) play a role in neuronal development by regulating the growth and morphology of microtubule structures. You are interested in studying the biochemical characteristics of a protein called “MAP2c”, which means that you need to purify it in an active form. Thus far, you have been able to able to isolate a mixture known as “microtubule protein”, which includes the...
I just want to see if the answers are right, so for 1a. since the microtubule...
I just want to see if the answers are right, so for 1a. since
the microtubule is in a cell that's in G0, would there be no
movement since everything stops in G0 phase? Or are the
microtubules continously depolymerizing/polymerizing at a constant
rate?
For 1b. I said the same thing since the cell is in G0 phase then
it wouldn't matter if it was microtubule treadmilling, it wouldn't
be moving.
1c. I'm not sure what exactly would happen
I'm...
You want to understand the role of dynein in microtubule transport in a newly discovered species...
You want to understand the role of dynein in microtubule transport in a newly discovered species of parasitic fungus. To do this, you chemically induce the fusion of a dynein adaptor protein to cargo vesicles that are marked with GFP (leading to the rapid recruitment and activation of the Dynein motor complex). You notice that after several minutes these GFP- vesicles accumulate on the periphery of the cell and that by time-resolved microscopy, most vesicles seem to be moving away...
You want to create an anti-cancer drug that destabilizes microtubules, hoping to prevent cell division in...
You want to create an anti-cancer drug that destabilizes microtubules, hoping to prevent cell division in the cancer cell line that you are studying. Which of the following drugs would enhance microtubule shrinkage and, therefore, utilize this mechanism of action? Answers A-D A a drug that inhibits GTP hydrolysis by the B-subunit in the GTP cap O B a drug that increases the ability of a tubulin dimer to bind to y-tubulin of the centrosome с a drug that increases...
You have discovered a single cellular eukaryotic organism that has very little vesicle traffickin...
You have discovered a single cellular eukaryotic organism that has very little vesicle trafficking. You suspect that this may be due to the relatively few formed microtubules that are observed in this species. Upon close examination, you find the microtubules that are present are unusually stable. When looking at an amino acid comparison with human alpha and beta tubulin, you notice that the alpha tubulin is identical, but the beta tubulin is different in the region responsible for GTP hydrolysis....
Name 2ors L! You are inte finding protein are interested in understanding how Top5 expression is...
Name 2ors L! You are inte finding protein are interested in understanding how Top5 expression is regulated. Top5 is a microtubule protein. You study a cell line where Top5 expression is controlled by a signal, Ligl. When hinds to and activates the membrane bound recentor it activates the Ras protein, which activates atein kinase called PKF, which then phosphorylates Grp4 on T224. Grp4 is a gene regulatory Wotein that can only enter the nucleus when phosphorylated: Thos is not expressed...
How do you elute proteins from an affinity column where the protein is bound to a...
How do you elute proteins from an affinity column where the protein is bound to a ligand which is attached to beads? Add a large amount of the free ligand that specficially binds the protein to compete for binding to the protein. Add SDS to denature the proteins. Add increasing amounts of salt to compete for ionic bonds with the protein. Wash the column with a large amount of buffer so that even the smallest molecules can filter through.
14. You are studying a newly discovered growth factor. You find that this growth factor stimulates...
14. You are studying a newly discovered growth factor. You find that this growth factor stimulates the proliferation of cells grown in the laboratory. You have also found that the receptor that binds the growth factor is a receptor kinase that activates Ras, which activates the MAP kinase pathway. Which mutations affecting this growth factor pathway would you expect to promote uncontrolled cell proliferation? Select all that apply. A. a mutation that inactivates the phosphatase that dephosphorylates the activated receptor...
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein...
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein - that is, its overall shape and how the chains are "folded” around each other - is very important for its function. In an aqueous environment, in an active, folded state the hydrophilic amino acids in the protein are facing outwards exposed to the water and the hydrophobic amino acids are hidden away from the water in the core of the protein. In a...
I just want to see if the answers are right, so for 1a. since
the microtubule is in a cell that's in G0, would there be no
movement since everything stops in G0 phase? Or are the
microtubules continously depolymerizing/polymerizing at a constant
rate?
For 1b. I said the same thing since the cell is in G0 phase then
it wouldn't matter if it was microtubule treadmilling, it wouldn't
be moving.
1c. I'm not sure what exactly would happen
I'm...
You want to create an anti-cancer drug that destabilizes microtubules, hoping to prevent cell division in the cancer cell line that you are studying. Which of the following drugs would enhance microtubule shrinkage and, therefore, utilize this mechanism of action? Answers A-D A a drug that inhibits GTP hydrolysis by the B-subunit in the GTP cap O B a drug that increases the ability of a tubulin dimer to bind to y-tubulin of the centrosome с a drug that increases...
Name 2ors L! You are inte finding protein are interested in understanding how Top5 expression is regulated. Top5 is a microtubule protein. You study a cell line where Top5 expression is controlled by a signal, Ligl. When hinds to and activates the membrane bound recentor it activates the Ras protein, which activates atein kinase called PKF, which then phosphorylates Grp4 on T224. Grp4 is a gene regulatory Wotein that can only enter the nucleus when phosphorylated: Thos is not expressed...
How do you elute proteins from an affinity column where the protein is bound to a ligand which is attached to beads? Add a large amount of the free ligand that specficially binds the protein to compete for binding to the protein. Add SDS to denature the proteins. Add increasing amounts of salt to compete for ionic bonds with the protein. Wash the column with a large amount of buffer so that even the smallest molecules can filter through.
6) Proteins are composed of amino acids polymerized into long chains. The structure of a protein - that is, its overall shape and how the chains are "folded” around each other - is very important for its function. In an aqueous environment, in an active, folded state the hydrophilic amino acids in the protein are facing outwards exposed to the water and the hydrophobic amino acids are hidden away from the water in the core of the protein. In a...
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