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44 Cards in this Set
- Front
- Back
In protein-protein interaction what is bound on cell surface?
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receptor bonded hormone (like adreniline for fight or flight response)
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In what interaction is PKA? What does PKA stand for?
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Protein-Protein, protein kinase A
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1. Receptor binds hormone which 2. activates GTP binding protein 3.which activates adenyl cyclase 4.which mediates the reaction is the process of what?
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Protein-protein interactions.
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What is C?
What is R? Where are these processes relevant? |
C is the catalytic subunit of protein kinase A
R is the regulatory subunit that releases C when bound to cAMP These processes happen in protein-protein interactions. |
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Glycogen phosphorase can be activated in minutes to make what for what?
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ATP for muscles
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C does what to many different proteins such as transcription factors, metabolic enzymes, etc.?
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phosphorylate
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cAMP-->AMP by what?
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enzyme phosphodiesterase (inhibited by caffiene-like compounds)
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What happens when there is a decrease in [cAMP]?
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C re-associates with R and becomes inactive
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Protein phosphates dephosphorylate what?
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PKA substrates of another area of regulation
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CREB is a transcription factor that does what?
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when phospholated by PKA it binds to specific sequences in promoters of responsive genes to regulate transcription.
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PKA phosphorylates Phosphorylase kinase and glycogen synthase to do what?
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PKA makes Phosphorylase kinase active an glycogen synthase inactive
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PKA phosphorylates Phosphorylase kinase and glycogen synthase to do what?
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PKA makes Phosphorylase kinase active an glycogen synthase inactive
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What activates glycogen phosphorylase ?
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phosphoroylase kinase
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Glycogen phosphorylase mediates the first step in glycolysis and ATP production which is
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glycogen to glucose-1-phosphate
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The activation of PKA promotes what? and inhibits what?
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promotes glycolysis and inhibits glycogen synthesis
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G proteins are slang for what?
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GTP-binding proteins.
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Guanine nucleotide binding are consider what?
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binary switches for GTP-bound ON and GDP-bound OFF.
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stimulation of exchange of GDP for GTP (from off to on) is activated by which protein?
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GNRPs protein
Guanine Nucleotide Release Proteins(lacking guanine nucleotide next) |
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What protein is turned on to bind guanine nucleotide sites to turn the G-site on?
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effector protein
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GAPs stands for what? GAPs do what?
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GTPase Activating Proteins, they convert bound GTP to GDP and PI and turn themselves off after interacting with the effector.
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What are the three subunit classes in trimetric G-proteins?
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alpha, beta, gamma
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Which of the three membrane anchors do most of the work?
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Alpha anchors
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A common example of loe molecular weight GTP binding proteins associated with tumors is
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ras is found in 30-50% of tumors in humans, other family members are rho, rab, ran
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Why do proteins degrade? Which protein does not turn over?
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Proteins degrade because they are starved for amino acids, histones don't turn over
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How long do histones last? How about regulatory proteins? Which proteins are most targeted or destruction?
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Histones (certain lens proteins) can last for years, regulatory proteins last for minutes to hours, damaged/misfolded/aged proteins are the most targeted for destruction
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What are three ways proteins are recognized to be destroyed?
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1. exposed hydrophobic domains
2. N-termini correlate with degregation 3. destruct box aa concentration |
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Destruct box PEST hypothesis is what?
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sequence rich in Pro, Glu, Ser, Thr
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Pro, Glu, Ser, Thr maybe the site of phosphorylation involved in what?
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Degregation, clone and mutate,
or mutate and delete to find rate |
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ubiquitin does what?
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conjugates enzymes in the protein destruction process
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What does ubiquitin ligase do?
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Adds more ubiquitin and makes a polyubiquitin chain and convalently attaches a side chain of lymine to make a branch chain polypeptide
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What continues to be polynuclated on a polynucleated substate
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ubiquitin
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What is the destruction machinery what takes place there?
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the Proteosome is where proteolous takes place
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What are five basics of the Proteosome?
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1. large (26S) complex in cyto,
2. recognizes polyubiquitin- conjugated proteins, 3. feeds proteins through with ATP-dependant unfoldase (sent to core of proteosome) 4. ubiquitin is released to be reused (cleaved off ) 5. protein degregation down to aa and small pepties |
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Immunity regulation includes what two things
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degradation and protein-protein interaction
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In B-lymphocytes NF-kB is what?
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an inactive transcription factor that binds IkB in the cytoplasm
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Activation of a protein kinase that phosphorylates IkB happens in what kind of cell?
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B-cells (antigen-presenting cells)
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Phosphorylated IkB is targeted by what?
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ubiquitin-conjugating enzymes
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What produces signaling proteins which are released into the blood to activate T-cells?
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NF-kB translocates to the nucleous to activate these genes to produce the proteins.
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What produces signaling proteins which are released into the blood to activate T-cells?
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NF-kB translocates to the nucleous to activate these genes to produce the proteins.
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What produces signaling proteins which are released into the blood to activate T-cells?
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NF-kB translocates to the nucleous to activate these genes to produce the proteins.
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By binding a calcium-binding protein called calmodulin a phosphatase is activated when what happens?
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T-cells become activated
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By binding a calcium-binding protein called calmodulin a phosphatase is activated when what happens?
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T-cells become activated
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By binding a calcium-binding protein called calmodulin a phosphatase is activated when what happens?
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T-cells become activated
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What produces signaling proteins which are released into the blood to activate T-cells?
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NF-kB translocates to the nucleous to activate these genes to produce the proteins.
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