Question 1
Question
5% of the human genome is genes that add a phosphate to something using ATP (Kinases)
Question 2
Question
Which of the following residues can be phosphorylated by kinases?
Answer
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Serine
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Threonine
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Tyrosine
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Valine
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Argenine
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Glutamic Acid
Question 3
Question
How many different kinases are there (roughly)?
Question 4
Question
In kinases, DFG & RC motifs are highly conserved
Question 5
Question
Which domains are commonly found in kinase interacting proteins?
Question 6
Question
SH3 proteins mediate the assembly of proteins structures by binding to proline rich peptides in them
Question 7
Question
SH domains modulate protein interactions by recognizing and binding to specific proteins by identifying specific peptide sequences
Question 8
Question
What is the role of PH domains?
Answer
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Binding the protein to the ER membrane
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Binding the protein to the cell membrane
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Binding the protein to nuclear membrane
Question 9
Question
Membranes form what?
Question 10
Question
What mediate membrane functions?
Question 11
Question
Mitochondiral membranes contail the most proteins, plasma membranes contain the least (Out of Mitochondrial, Plasma and Myelin membranes)
Question 12
Question
Most integral membrane proteins span the membrane
Question 13
Question
Integral proteins interact extensively with what?
Answer
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The hydrocarbon chains of lipids
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The phosphate groups of phospholipids
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The hydrocarbon tails of phospholipids
Question 14
Question
Peripheral proteins are bound to the membrane via the head groups of phospholipids
Question 15
Question
How do we tell how strongly a membrane protein is associated?
Question 16
Question
Baterial Rhodopsin uses heat to pump protons out of the membrane
Question 17
Question
How is the hydrophobic core formed in baterorhodopsin?
Question 18
Question
In the case of the highly conserved 'Membrane Spanning Alpha Helix Structure', what must be on the outside?
Answer
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Phospholipids
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Non-polar aa
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Polar aa
Question 19
Question
The membrane spanning alpha helix structure acts as what?
Question 20
Question
Transmembrane helices can be predicted by a long string (or more) of hydrophobic amino acids in their aa sequence
Question 21
Question
What is used to estimate the free energy change of a residue on transfer of a residue to water (i.e. how much energy does it take to disassociate the aa from the protein)?
Answer
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A polarity scale
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An amino scale
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A pH scale
Question 22
Question
An amino acid with high energy lies buried in a hydrophobic region i.e. the membrane
Question 23
Question
How large is the hydrocarbon core of the membrane?
Question 24
Question
What is the name of the 20aa section of an integral protein that spans the membrane?
Question 25
Question
How is a Hydropathy plot formed?
Answer
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The free energy change for each 20 aa segement plotted against the first aa in each segment
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The free energy change for each 20 aa segement plotted against the last aa in each segment
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The free energy change for each 30 aa segement plotted against the first aa in each segment
Question 26
Question
What is the point of a hydropathy plot?
Answer
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To find which aa are in hydrophobic areas
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To find the window of integral proteins
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To find the window of peripheral proteins
Question 27
Question
The criterion level for a hydropathy plot is +68
Question 28
Question
What is Porin an example of?
Answer
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Membrane spanning alpha helices
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Membrane spanning beta sheets
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Membrane spanning helix/beta sheet structure
Question 29
Question
What tends to be the features of membrane spanning beta sheet residues?
Question 30
Question
The polarity of the internal aa in a membrane spanning beta sheet depends on the size
Question 31
Question
Each sheet in the m.s beta sheet arrangement is hydrogen bonded to its neighbor in a parallel manner