Explore the functions of cytoskeletal elements in this quiz. Topics include vesicle formation, phospholipid bilayer asymmetry, and the roles of microfilaments and GTP-binding proteins. Ideal for students enhancing their understanding of cellular structure and dynamics.
Liposomes cause the protein to denature
The protein is involved in the initiation of vesicle formation.
The protein is involved in liposome denaturation
The protein triggers protein synthesis.
The protein causes the entry of water into the liposomes
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It is initially established in the Golgi complex during lipid and protein modification
It is initially established in the ER during lipid and protein synthesis.
It is initially established in the secretory vesicles during lipid and protein modification
It is initially established in the mitochondria by random insertion into the membranes.
All of the above
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Microfilaments
Microtubules
Intermediate filaments
All of the above
Macrofilaments
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Proteins that are to remain in the cytosol
Peripheral proteins of the inner cell membrane surface
Peripheral proteins of the outer cell membrane surface
Proteins to be transported to the nucleus
A, b and d
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AP2
GGA
Clathrin
Dynamin
Opsonin
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Medial endosomes
Late endosomes
Early lysosomes
Medial lysosomes
Early endosomes
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Nothing - the sequence is random
The spatial arrangement of specific glycosyltransferases that contact proteins as they pass through the Golgi complex
The concentration of sugars in the Golgi complex
The sequence of sugars in the Golgi complex
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The cisternal maturation model
The cargo carrying model
The vesicular transport model
The secretory transport model
The chemiosmotic model
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It has a large surface area allowing the attachment of many ribosomes
The ER cisternae lumen favors the folding and assembly of proteins.
The RER segregates secretory, lysosomal and plantcell vacuolar proteins from other newly made proteins, allowing their modification, and sends them to their destination.
A and c
A, b and c
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In a retrograde direction
Toward the plus-end of the microtubule
In an anterograde direction
Towards the fastest growing end of the microtubule
C and d
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The similarity of kinesin-like protein heads and the variation in their tails are purely random.
The similarity of the heads is explained by their similar roles in interacting with microtubules; the variation in the tails reflects the variety of cargoes to which they bind.
The similarity of the heads is explained by their different roles in interacting with microtubules; the variation in the tails reflects the similar cargoes to which they bind.
The similarity of the heads is explained by their similar roles in interacting with microtubules; the variation in the tails reflects the similar cargoes to which they bind
The similarity of the heads is explained by their different roles in interacting with microtubules; the variation in the tails reflects the variety of cargoes to which they bind
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Microfilments
Microtubules
Intermediate filaments
All of the above
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Endocytosis
Rabs
GTP binding proteins
T-snares
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Luminal, lipid
Cytosolic, lipid
Cytosolic, carbohydrate
Luminal,protein
Cytosolic, protein
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Endocytosis
Phagocytosis
Autophagy
Exocytosis
Pinocytosis
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Signal recognition particle, DNA and protein
Signal recognition particle, carbohydrate and protein
SRP and its components, RNA and protein.
SRP and its components, RNA and protein.
Signal recognition protein, carbohydrate and lipid
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Actin
Myosins
Tubulin
Dynein
Kinesin-like proteins
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COPI-coated vesicles move materials from Golgi to the secretory vesicle
Tethering proteins mediate docking between target and vesicle
COPII-coated vesicles move materials from ER to Golgi
Movement may be mediated by microtubules
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The polysomal response
The posttranscriptional response
The unfolded protein response (UPR)
The proteasomal response
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They electromagnetically attract the correct cargo proteins.
The coats have a specific affinity for the cytosolic tails of integral membrane receptors for cargo proteins that reside in the donor membrane.
The coats have a specific affinity for the luminal tails of integral membrane
Receptors for cargo proteins that reside in the donor membrane.
The coat proteins directly attach to the cargo proteins in the lumen of the forming vesicles.
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Excessive
Progressive
Excessive
Processive
Aggressive
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They stabilize microtubules
They encourage depolymerization
They cause polymerization.
They block other kinesins from moving along microtubules.
They add phosphate groups to tubulin
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Receptor up-regulation
Receptor annihilation
Endocytic assignation
Receptor down-regulation
Super signaling
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Inner peripheral membrane proteins
Soluble lysosomal proteins
Vacuolar enzymes
Proteins of the extracellular matrix
All of the above
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With over 60 Rab genes identified in humans, Rabs constitute the most diverse group of proteins involved in membrane trafficking.
Rabs have the potential of giving each cell compartment a unique surface identity
Different Rabs have been found to be associated with different membrane compartments
The preferential localization of Rabs would allow them to recruit the various proteins involved in targeting specificity.
All others are correct.
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The protons move into the intermembrane space in chloroplasts and into the thylakoid lumen in mitochondria.
In mitochondria, the force is expressed primarily as an electrochemical potential; in chloroplasts, it is largely, if not exclusively, due to a pH gradient.
The protons move into the stroma in chloroplasts and out of the mitochondria
In mitochondria, the force is expressed primarily as a pH gradient; in chloroplasts, it is largely, if not exclusively, due to an electrochemical potential
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Reduction of oxygen, oxidation of NADPH, formation of ATP
Oxidation of water, reduction of NADP+ , formation of ATP
Oxidation of water, recuction of NADP+ , hydrolysis of ATP
Fixation of carbon dioxide, release of oxygen, synthesis of glucose
Release of oxygen, fixation of carbon dioxide, hydrolysis of ATP
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A cluster of manganese ions
A cluster of 4 manganese ions and one calcium ion
A cluster of iron ions
A cluster of magnesium ions
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It might deactivate them
It might activate them
It might split them in two pieces
B and c are correct
None of the above
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CO2 and O2 bind to a regulatory site instead of the active site.
Rubisco binds to a regulatory site.
Both CO2 and O2 bind directly to Rubisco's active site.
CO2 and O2 bind to RuBP, which occupies the active site; their ability to attack RuBP is roughly equal.
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Stroma
Thylakoid membrane
Cytosol
Lumen
Grana
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As a response to mitochondria ATP generation
When water is split during the generation of CO2
When a proton moves from the stroma to plastoquinol in the thylakoid membrane
When a proton leaves the thylakoid to the stroma
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Oxygen
Carbohydrates
Both carbohydrates and oxygen
Water
Carbon dioxide
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Endosome
Secretory vesicle
Lysosome
Golgi apparatus
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The appropriate signal sequence is present
Mannose-6-phosphate is added to the protein.
The yeast cell is capable of phagocytosis
Plenty of clathrin-coated pits may be formed.
All of the above
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Constitutive secretion
Phagocytosis.
Regulated secretion.
The formation of clathrin-coated pits.
The mucus response
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Protein possesses a signal for localization within the Golgi apparatus
Protein does not possess a signal peptide for localization within the lumen of the rough endoplasmic reticulum.
Protein was not translated by the ribosomes.
Secretory vesicles are not fusing with the plasma membrane
All of the above
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Chloroplasts
Peroxisomes.
The Golgi apparatus
Mitochondria
Lysosomes.
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Carbon dioxide
Water
Oxygen
Glucose
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Yellow
All colors including yellow
All colors except yellow
No colors are absorbed; they are only scattered
It cannot be determined from the given information
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True
False
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Directly phosphorylates ATP to ADP
Increases the binding affinity of the active site for the ATP product
Directly phosphorylates ADP to ATP
Directly phosphorylates ATP to ADP
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ATP synthesis continues
All the b(beta)-subunits will be in the same conformation
The b(beta)-subunits will be in different conformations and will change as normal
The b(beta)-subunits will be in different conformations and will not change as normal
None of the above
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Has a very low affinity for nucleotides
A and e
Has a very low affinity for proteins
Binds ATP, ADP and inorganic phosphate groups tightly
Very tightly binds ADP and an inorganic phosphate group
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They diffuse freely into the luminal leaflet
There are enzymes called flippases that flip these lipids later into the opposite leaflet
They are disassembled on the cytoplasmic side and reassembled on the luminal side.
They move to the cytoplasmic leaflet by osmosis
There are enzymes called translocases that flip these lipids later into the opposite leaflet
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Selected Calvin cylce enzymes are immobilized at night
Selected Calvin cycle enzymes are inactive in the dark because thioredoxin is oxidized
Selected Calvin cycle enzymes are inactive in the dark because they denature at night
Chloroplasts shrink at night
Selected Calvin cycle enzymes are inactive in the dark because thioredoxin is reduced
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Protons follow a linear path during the process
Electrons follow a circular path during the process
Protons originate in PSI and end up there after passage from molecule to molecule
Move protons against their gradient
Electrons leave PSI after light absorption, flow through a number of proteins and end up back in PSI
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Attach the phosphate group to ADP
Attach the phosphate group to ATP
Release the tightly bound ATP from the ATP synthase catalytic site
Attach the tightly bound ATP to the ATP synthase catalytic site
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