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BIOL_V
200 CH 4
Final exam
with 100%
accurate
solutions
(GUARAN
TEED
SUCCESS)
bio final ch 4
Problem 4.1.2
(tags: #protein targeting, #KDEL, #NLS, #M6P, #prediction)
Where would you expect to find a genetically engineered
fluorescent protein that contains the following signals? How
are these signals used by the cell to maintain these proteins
in their proper locations?
a) An N-terminal signal sequence, an internal 'Stop' sequence
and an NLS.
b) Only a KDEL sequence.
c) An N-Terminal signal sequence, and a protein sequence
indicating the addition of an M6P oligosaccharide.
d) No sorting signals.
Problem 4.1.4
(tags: #protein topology, #signal sequence, #transfer sequence)
Match the following arrangements of proteins in the membrane with the
appropriate polypeptide domain maps below:
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Protein Maps Domain Maps
Cisterna
1
3
Problem 4.1.5
(tags: #hydrophobicity plots, #protein
topology)
The figure on the right is an average
hydrophobicity plot for a protein. The N-
terminal end is amino acid number 1 .
Given that amino acid 1 represents the
first codon of the open reading frame for
this protein, sketch the following:
a) The domain map for the protein.
b) The arrangement of this protein in the
membrane. Be sure to label the N-
terminal and C-terminal ends of the
protein, and the cytosol and lumen
sides of the membrane.
50 100 150 200 250
Amino Acid Number
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Problem 4.1.7
(tags: #SDS-PAGE, #protein topology, #experimental controls, #protein
glycosylation)
Co-translational insertion of proteins into the ER can be studied in a
cell-free system that uses small enclosed segments of rough ER
(called microsomes) in a test tube.
TREATMENT
Researchers studied whether a protein was
undergoing co-translational insertion into protease
the ER. The mRNA was allowed to detergent
translate in the cell-free system, in the
endo
presence or absence of microsomes, treated
in 4 different ways: H
No treatment
Addition of a protease to the cell-free AcD-
system
1 2345 6 78
Addition of a protease and detergent to
the cell-free system
Addition of Endo H (enzyme that removes polysaccharides) in a
way that allows Endo H to pass through the microsomal membrane
The resulting proteins were then subjected to SDS-
PAGE, and the results are shown in the image
above.
a) Describe what you observe in each lane of the gel.
Include which lanes are controls, and what they are controlling for.
b) Co-translational insertion of proteins into the rER microsomes can be
judged by several criteria, including:
• Whether the newly synthesized proteins are protected from
proteases added to the test tube,
• Whether the newly synthesized proteins are glycosylated by ER
enzymes,
• Whether the signal peptide is cleaved by ER-localized signal
peptidase.
Using these 3 criteria, draw a conclusion about whether this protein
is co-translationally inserted into the rER microsomes or not.
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BIOL_V
200 CH 4
Final exam
with 100%
accurate
solutions
(GUARAN
TEED
SUCCESS)
bio final ch 4
Problem 4.1.2
(tags: #protein targeting, #KDEL, #NLS, #M6P, #prediction)
Where would you expect to find a genetically engineered
fluorescent protein that contains the following signals? How
are these signals used by the cell to maintain these proteins
in their proper locations?
a) An N-terminal signal sequence, an internal 'Stop' sequence
and an NLS.
b) Only a KDEL sequence.
c) An N-Terminal signal sequence, and a protein sequence
indicating the addition of an M6P oligosaccharide.
d) No sorting signals.
Problem 4.1.4
(tags: #protein topology, #signal sequence, #transfer sequence)
Match the following arrangements of proteins in the membrane with the
appropriate polypeptide domain maps below:
FOR MORE EXAMS
EMAIL:
,FOR MORE EXAMS
EMAIL:
Protein Maps Domain Maps
Cisterna
1
3
Problem 4.1.5
(tags: #hydrophobicity plots, #protein
topology)
The figure on the right is an average
hydrophobicity plot for a protein. The N-
terminal end is amino acid number 1 .
Given that amino acid 1 represents the
first codon of the open reading frame for
this protein, sketch the following:
a) The domain map for the protein.
b) The arrangement of this protein in the
membrane. Be sure to label the N-
terminal and C-terminal ends of the
protein, and the cytosol and lumen
sides of the membrane.
50 100 150 200 250
Amino Acid Number
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EMAIL:
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Problem 4.1.7
(tags: #SDS-PAGE, #protein topology, #experimental controls, #protein
glycosylation)
Co-translational insertion of proteins into the ER can be studied in a
cell-free system that uses small enclosed segments of rough ER
(called microsomes) in a test tube.
TREATMENT
Researchers studied whether a protein was
undergoing co-translational insertion into protease
the ER. The mRNA was allowed to detergent
translate in the cell-free system, in the
endo
presence or absence of microsomes, treated
in 4 different ways: H
No treatment
Addition of a protease to the cell-free AcD-
system
1 2345 6 78
Addition of a protease and detergent to
the cell-free system
Addition of Endo H (enzyme that removes polysaccharides) in a
way that allows Endo H to pass through the microsomal membrane
The resulting proteins were then subjected to SDS-
PAGE, and the results are shown in the image
above.
a) Describe what you observe in each lane of the gel.
Include which lanes are controls, and what they are controlling for.
b) Co-translational insertion of proteins into the rER microsomes can be
judged by several criteria, including:
• Whether the newly synthesized proteins are protected from
proteases added to the test tube,
• Whether the newly synthesized proteins are glycosylated by ER
enzymes,
• Whether the signal peptide is cleaved by ER-localized signal
peptidase.
Using these 3 criteria, draw a conclusion about whether this protein
is co-translationally inserted into the rER microsomes or not.
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EMAIL:
