BIOL 314 Final Flashcards
Maintaining pH and salt concentrations is critical to keeping proteins functional. What is the molecular mechanism by which pH affects protein function?
-Only the primary structure is altered, which changes the folding and function of the protein.
-A few of the polar R-groups can change charge, and the new attraction or repulsion can alter the shape of the protein.
-The hydrogen bonds within the polypeptide backbone that form the secondary structures are completely disrupted.
-The N- and C-terminus amino acids with their amino and carboxyl ends can change the shape of the entire protein.
A few of the polar R-groups can change charge, and the new attraction or repulsion can alter the shape of the protein.
Which of the following is NOT a feature commonly observed in α helices?
-cylindrical shape
-left-handedness
-1 helical turn every 3.6 amino acids
-amino acid side chains that point outward
left-handedness
Two or three α helices can sometimes wrap around each other to form coiled-coils. The stable wrapping of one helix around another is typically driven by __________ interactions.
hydrophilic
hydrophobic
ionic
van der Waals
hydrophobic
The three-dimensional coordinates of atoms within a folded protein are determined experimentally. After researchers obtain a protein’s structural details, they can use different techniques to highlight particular aspects of the structure. What visual model best displays a protein’s secondary structures (α helices and β sheets)?
space-filling
ribbon
backbone
wire
ribbon
Cyclic AMP (cAMP) is a small molecule that associates with its binding site with a high degree of specificity. Which types of noncovalent interactions are the most important for providing the “hand in a glove” binding of cAMP?
hydrophobic interactions
electrostatic interactions
hydrogen bonds
van der Waals interactions
hydrogen bonds
Some proteins have α helices, some have β sheets, and still others have a combination of both. What makes it possible for proteins to have these common structural elements?
specific amino acid sequences
side-chain interactions
the hydrophobic-core interactions
hydrogen bonds along or between strands of the protein backbone
hydrogen bonds along or between strands of the protein backbone
The variations in the physical characteristics between different proteins are influenced by the overall amino acid compositions, but even more important is the unique amino acid
sequence.
bond.
number.
orientation.
sequence
Proteins bind selectively to small-molecule targets called ligands. The selection of one ligand out of a mixture of possible ligands depends on the number of weak, noncovalent interactions in the protein’s ligand-binding site. Where is the binding site typically located in the protein structure?
buried in the interior of the protein
on the surface of the protein
inside a cavity on the protein surface
on the surface of the protein in the presence of ligand
inside a cavity on the protein surface
In the polypeptide sequence shown below, which letter represents the peptide bond?
bond between c=o and n-h bonds, removes the h from nh2 and oh from cooh to form bond
Figure 4-2
C
A
B
D
C
Complete the sentence with the best option provided below. The primary structure of a protein is the
lowest energy conformation.
amino acid sequence.
amino acid composition.
average size of amino acid side chains.
amino acid sequence
A lab has sequenced a novel cancer-causing gene in humans. What can we learn from the protein sequence by inputting the predicted protein sequence into a computer and conducting bioinformatic analysis?
the rate at which the protein will be degraded
how many protein-binding partners it will have, including its quaternary structure
the complete tertiary structure of this protein
how to predict the domains by matching the amino acids with another similar sequence
how to predict the domains by matching the amino acids with another similar sequence
Polypeptides are synthesized from amino acid building blocks. The condensation reaction between the growing polypeptide chain and the next amino acid to be added involves the loss of a(n)
carbon atom.
carboxylic acid group.
water molecule.
amino group.
water molecule
Cells utilize several mechanisms for restricting the movement of membrane proteins within the plasma membrane. One of these mechanisms allows cells to form specialized attachment structures called focal adhesions to promote cell motility. Which of the following mechanisms describes how motile cells form focal adhesions on the plasma membrane?
Proteins are tethered to the cell cortex.
Proteins are tethered to the proteins on the surface of another cell.
Proteins are tethered to the extracellular matrix.
Protein movement is limited by the presence of a diffusion barrier.
Proteins are tethered to the extracellular matrix.
Which of the following types of lipids is the most abundant in the plasma membrane?
phospholipids
sterols
triacylglycerides
glycolipids
phospholipids
Porin proteins form large, barrel-like channels in the membrane. Which of the following statements about these channels is FALSE?
They are made primarily of β sheets.
They cannot form narrow channels.
They have alternating hydrophobic and hydrophilic amino acids.
They are made primarily of α helices.
They are made primarily of α helices.
New membrane phospholipids are synthesized by enzymes bound to the __________ side of the __________ membrane.
luminal; Golgi
cytosolic; mitochondrial
cytosolic; endoplasmic reticulum
extracellular; plasma
cytosolic; endoplasmic reticulum
Consider a transport vesicle containing a membrane glycoprotein. The glycoprotein and the vesicle’s phospholipids are delivered to the plasma membrane, as shown in the figure below. Which of the following is an accurate description of the outcome of this process?
Figure 11-4
-The portion of the glycoprotein that was inside of the vesicle ends up in the cytosol after it is delivered to the plasma membrane.
-Some of the individual phospholipid molecules are released into the cytosol to prevent the plasma membrane, and thus the cell, from becoming too large.
-The phospholipids that are delivered to the noncytosolic face of the plasma membrane used to be in the interior (luminal) face of the vesicle.
-The fusion event between the vesicle and the plasma membrane randomizes the phospholipids between the cytosolic and noncytosolic faces of the bilayer.
The phospholipids that are delivered to the noncytosolic face of the plasma membrane used to be in the interior (luminal) face of the vesicle.
Which of the following is most likely to occur after the lipid bilayer is pierced?
The membrane expands.
The membrane reseals.
A tear forms.
The membrane collapses.
The membrane reseals
Which of the following substances is most commonly used to help purify a membrane protein?
sucrose
ethanol
high salt solution
detergent
detergent
Cholesterol serves several essential functions in mammalian cells. Which of the following is NOT influenced by cholesterol?
membrane permeability
membrane fluidity
membrane thickness
membrane rigidity
membrane thickness
Cells utilize several mechanisms for restricting the movement of membrane proteins within the plasma membrane. One of these mechanisms allows cells to present antigens to other cells to trigger the adaptive immune response. Which of the following mechanisms describes how antigen-presenting cells perform this function?
Proteins are tethered to the cell cortex.
Proteins interact with the proteins on the surface of another cell.
Protein movement is limited by the presence of a diffusion barrier.
Proteins are tethered to the extracellular matrix.
Proteins interact with the proteins on the surface of another cell. (other cells)
A bacterium is suddenly expelled from a warm human intestine into the cold world outside. Which of the following adjustments might the bacterium make to maintain the same level of fluidity in its cell (plasma) membrane?
decrease the amount of cholesterol in the membrane
add lipids with hydrocarbon tails that are shorter and have more double bonds
add lipids with hydrocarbon tails that are longer and have fewer double bonds
decrease the number of glycolipids in the membrane
add lipids with hydrocarbon tails that are shorter and have more double bonds
Voltage-gated channels contain charged protein domains, which are sensitive to changes in membrane potential. By responding to a threshold in the membrane potential, these voltage sensors trigger the opening of the channels. Which of the following best describes the behavior of a population of channels exposed to such a threshold?
All channels open completely.
A few channels remain closed and most open completely.
All channels open partly, each to a different degree.
All channels open partly, to the same degree.
A few channels remain closed and most open completely
Which of the following occur without coupling transport of the solute to the movement of a second solute?
the export of Na+ from cells to maintain resting membrane potential
export of Ca2+ from the cytosol
export of H+ from animal cells for pH regulation
export of glucose out of gut epithelial cells
export of glucose out of gut epithelial cells
Some cells express aquaporin proteins—they are channel proteins that facilitate the flow of water molecules through the plasma membrane. What regulates the rate and direction of water diffusion across the membrane?
resting membrane potential
aquaporin conformation
availability of ATP
the concentration of water on either side of the membrane
the concentration of water on either side of the membrane
If the K+ concentration increases in extracellular space, the membrane potential of a cell will become
repolarized.
hyperpolarized.
depolarized.
stabilized, because the membrane is not permeable to K+.
depolarized.
Transporters, in contrast to channels, work by
filtering solutes by size.
specific recognition of transport substrates.
filtering solutes by charge.
a gating mechanism.
specific recognition of transport substrates.
Negatively charged ions are required to balance the net positive charge from metal ions such as K+, Na+, and Ca2+. Which of the following negatively charged ions is the most abundant outside the cell and which ion most often counterbalances the negative charge (written in parentheses)?
Cl- (Na+)
PO43- (K+)
PO43- (Ca2+)
Cl- (Ca2+)
Cl- (Na+)
Although the extracellular environment has a high sodium ion concentration and the intracellular environment has a high potassium ion concentration, both must be neutralized by negatively charged molecules. In the extracellular case, what is the principal anion?
OH-
HCO3-
Cl-
PO43-
Cl-
Pumps are transporters that can harness energy provided by other components in the cells to drive the movement of solutes across membranes, against their concentration gradient. This type of transport is called
free diffusion.
passive transport.
active transport.
facilitated diffusion.
active transport
If a chemical blocks the voltage-gated K+ channels in an action potential, which region of the action potential will be the most affected?
Figure 12-3
A
B
D
C
C (repolarization phase )
Active transport requires the input of energy into a system so as to move solutes against their electrochemical and concentration gradients. Which of the following is NOT one of the common ways to perform active transport?
K+-coupled
light-driven
ATP-driven
Na+-coupled
K+-coupled
As living cells grow and form complex communities in their environment, which statement describes entropy (or disorder) in a way that is consistent with the second law of thermodynamics?
The entropy inside the cell increases as cells grow.
The entropy in the environment decreases as cells grow.
The entropy in the environment increases as cells grow.
The entropy in the cells and the environment is unchanged as cells grow.
The entropy in the environment increases as cells grow.
Macromolecules in the cell can often interact transiently as a result of noncovalent interactions. These weak interactions also produce stable, highly specific interactions between molecules. Which of the factors below is the most significant in determining whether the interaction will be transient or stable?
the rate of synthesis
surface complementarity between molecules
the concentration of each molecule
the size of each molecule
surface complementarity between molecules
The synthesis of glutamine from glutamic acid requires the production of an activated intermediate followed by a condensation step that completes the process. Both amino acids are shown in Figure 3-4.
oh on glu switched for a nh2, acitvation step involves atp
Figure 3-4
Which molecule is added to glutamic acid in the activation step?
ADP
ATP
NH3
phosphate
ATP
Lysozyme is an enzyme that specifically recognizes bacterial polysaccharides, which render it an effective antibacterial agent. Into what classification of enzymes does lysozyme fall?
protease
nuclease
hydrolase
isomerase
hydrolase
Proteins can assemble to form large complexes that work coordinately, like moving parts inside a single machine. Which of the following steps in modulating the activity of a complex protein machine is LEAST likely to be directly affected by ATP or GTP hydrolysis?
translation of protein components
complex disassembly
conformational change of protein components
complex assembly
translation of protein components
Which of the following statements is true?
The sequence of the atoms in the polypeptide backbone varies between different proteins.
Nonpolar amino acids tend to be found in the interior of proteins.
There is free rotation around all covalent bonds in the polypeptide backbone.
Peptide bonds are the only covalent bonds that can link two amino acids in proteins.
Nonpolar amino acids tend to be found in the interior of proteins.
Which of the following statements is true?
Disulfide bonds stabilize but do not change a protein’s final conformation.
Disulfide bonds are formed mainly in proteins that are retained within the cytosol.
Disulfide bonds are formed by the cross-linking of methionine residues.
Disulfide bonds are more common for intracellular proteins, compared to extracellular proteins.
Disulfide bonds stabilize but do not change a protein’s final conformation.
The correct folding of proteins is necessary to maintain healthy cells and tissues. The presence of unfolded proteins is associated with some neurodegenerative disorders such as Alzheimer’s disease, Huntington’s disease, and Creutzfeldt–Jakob disease (the specific faulty protein is different for each disease). What happens to these disease-causing, unfolded proteins?
They form structured filaments.
They bind a different target protein.
They form protein aggregates.
They are degraded.
They form protein aggregates.
Which of the following statements is true regarding the behavior of lipids in cell membranes?
Membrane lipids diffuse laterally within the plane of the membrane.
The hydrocarbon tails of membrane lipids act like stiff rods.
Membrane lipids frequently flip-flop between one monolayer and the other.
Individual lipids tumble end over end within a single monolayer.
Membrane lipids diffuse laterally within the plane of the membrane.
Which of the following functions of the plasma membrane is possible without membrane proteins?
intercellular communication
import/export of molecules
cellular movement
selective permeability
selective permeability
How does a bilayer arrangement of phospholipids result in higher entropy for the system and thus make membrane formation energetically favorable?
Polar head groups form a hydrogen-bonding network at the interface with water.
Fatty acid tails are highly saturated and flexible.
Water molecules form cagelike structures around hydrophobic molecules, thus encouraging the latter to cluster together and limit their contact with water.
Hydrogen bonds form between neighboring polar head groups in the bilayer.
Water molecules form cagelike structures around hydrophobic molecules, thus encouraging the latter to cluster together and limit their contact with water.
Which of the following membrane lipids does not contain a fatty acid tail?
phosphatidylserine
a glycolipid
cholesterol
phosphatidylcholine
cholestrol
Which of the following mechanisms best describes the process by which nutrients are taken up selectively at the apical surface and then released from the basal and lateral surfaces of the epithelial cells that line the gut?
Proteins are tethered to the proteins on the surface of another cell.
Protein movement is limited by the presence of a diffusion barrier.
Proteins are tethered to the extracellular matrix.
Proteins are tethered to the cell cortex.
Protein movement is limited by the presence of a diffusion barrier.
Cells use membranes to help maintain set ranges of ion concentrations inside and outside the cell. Which of the following ions is the most abundant outside a typical mammalian cell?
Na+
K+
Cl-
Ca2+
Na+
The Na+-K+ pump has been inhibited in the gut epithelial cells with a chemical like ouabain. What will happen to glucose transport on the apical membrane, and why?
Glucose transport will stay the same, because the Na+ gradient is not involved in the transport of glucose.
Inward glucose transport will increase because the outward K+ electrochemical potential will decrease.
Inward glucose transport will slowly decrease into the epithelial cells because of the slow accumulation in intracellular Na+.
Inward glucose transport will increase because of the higher electrochemical potential of Na+.
Inward glucose transport will slowly decrease into the epithelial cells because of the slow accumulation in intracellular Na+.
Which of the following statements about resting membrane potential is true?
The resting membrane potential for most animal cells is zero mV, because the positive and negative ions are in balance.
The resting membrane potential for most animal cells is negative, because the inside of the cell is more negatively charged than the outside of the cell.
At the resting membrane potential, no ions enter or exit the cell.
The resting membrane potential for most animal cells is positive, because Na+ ions are so plentiful inside cells.
The resting membrane potential for most animal cells is negative, because the inside of the cell is more negatively charged than the outside of the cell.
Below is a list of molecules with different chemical characteristics. Knowing that all molecules will eventually diffuse across a phospholipid bilayer, select the option below that most accurately predicts the relative rates of diffusion of the following molecules (fastest to slowest):
alanine estrogen propanol sodium
sodium > propanol > alanine > estrogen
estrogen > propanol > sodium > alanine
alanine > propanol > sodium > estrogen
estrogen > propanol > alanine > sodium
estrogen > propanol > alanine > sodium
Coiled coils are defined by all of the following EXCEPT:
-Coiled coils are the hallmark of Alzheimer’s disease, forming the amyloid fibrils found in diseased brains.
-they coil together due to their amphipathic nature
-Two or even sometimes three heptad repeat coils wind together to form a superhelical bundle
-they are comprised of “heptad repeats” where the 1st and 4th amino acids are hydrophobic
Coiled coils are the hallmark of Alzheimer’s disease, forming the amyloid fibrils found in diseased brains.
Two or three α helices can sometimes wrap around each other to form coiled-coils. The stable wrapping of one helix around another is typically driven by
__________ interactions.
hydrophilic
ionic
van der Waals
hydrophobic
hydrophobic
Advantages of protein phosphorylation as a regulatory mechanism include all of
the following EXCEPT:
-It changes the chemical nature of S,T,Y, and H R-group sidechains from polar to basic in nature.
-It can trigger allosteric changes to alter activity
-Several different amino acids can be phosphorylated, meaning that a protein could be
regulated by different kinases and at different sites, increasing the potential complexity of
signaling
-Depending on the context, phosphorylation can be used to positively regulate or negatively regulate a protein
-It changes the chemical nature of S,T,Y, and H R-group sidechains from polar to basic in nature.
Regulation of a protein’s activity by the binding of a small nucleotide such as ATP or GTP has all of the advantages below EXCEPT:
-Its small size allows it to diffuse rapidly to the protein, a key advantage to speed up “multi-step” processes
-its binding can cause allosteric changes in the protein that regulate its activity
-it modifies a single amino acid on the protein it regulates, increasing the number of different options for regulatory complexity if it can bind more than one site
-it can positively or negatively regulate the protein’s interaction with other proteins, depending on the context
-it modifies a single amino acid on the protein it regulates, increasing the number of different options for regulatory complexity if it can bind more than one site
Fluorescence recovery after photobleaching (FRAP) is a way to measure:
Mobility of a protein within the cell
The free energy of a protein.
The equilibrium constant for a given reaction
Change in the membrane potential
Mobility of a protein within the cell
Membrane synthesis in the cell requires the regulation of growth for both halves of the bilayer and the selective retention of certain types of lipids on one side or the other. Which group of enzymes accomplishes both of these tasks?
phospholipases
flippases
convertases
glycosylases
flippases
Most animal fats form a solid at room temperature, while plant fats remain liquid at room temperature. Which of the following is a feature of lipids in plant membranes that best explains this difference?
higher levels of sterols
larger head groups
unsaturated hydrocarbons
longer hydrocarbon tails
unsaturated hydrocarbons
Which of the following statements is TRUE?
Membrane lipids diffuse within the plane of the membrane.
In eukaryotes, all membrane-enclosed organelles are surrounded by one lipid bilayer.
In an aqueous environment, the formation of liposomes by phospholipids requires energy.
Membrane lipids frequently flip-flop between one monolayer and the other
Membrane lipids diffuse within the plane of the membrane.
Membrane lipids are capable of many different types of movement. Which of these does not occur spontaneously in biological membranes?
rotation around the long axis of a fatty acid
moving between lipid layers
flexing of hydrocarbon chains
lateral movement
moving between lipid bilayers
Why does the part of the polypeptide chain that crosses the lipid bilayer of most transmembrane proteins usually exist as an alpha helix or beta barrel?
-Because a rigid structure such as occurs with these conformations is needed to penetrate through a lipid bilayer.
-Because in both an alpha helix or a beta barrel the polar peptide bonds of the polypeptide backbone chain are H-bonded and completely shielded from the hydrophobic
environment of the lipid bilayer by the hydrophobic amino acid side chains.
-Because these secondary structures always form the correct length needed to traverse a lipid bilayer (20-24 amino acids)
-Because both of these secondary structures are able to shield their polar groups away from the hydrophobic lipid bilayer due to the van der Waals forces.
Because in both an alpha helix or a beta barrel the polar peptide bonds of the polypeptide backbone chain are H-bonded and completely shielded from the hydrophobic
environment of the lipid bilayer by the hydrophobic amino acid side chains.
A similarity between symporters and antiporters is:
Both transporters are responsive to the membrane potential, opening once threshold is reached.
Both transporters couple the movement of two different solvents across the cell membrane.
Both transporters operate using passive transport mechanisms.
Both transporters are coupled to ATP hydrolysis to drive solute transport across the membrane.
2.5 ptsQuestion 36
free diffusion.
passive transport.
(Q013) Pumps are transporters that are able to harness energy provided by other
components in the cells to drive the movement of solutes across membranes,
against their concentration gradient. This type of transport is called
Both transporters couple the movement of two different solvents across the cell membrane.
A transporter protein that is also described as a “pump”:
Always hydrolyzes ATP to function
Is specialized to allow ions to move through an open pore in response to a signal that triggers an allosteric change that opens the pore.
Operates via a passive transport mechanism to transport solutes from high concentration to low.
uses energy to transport a solute against its concentration or electrochemical gradient
uses energy to transport a solute against its concentration or electrochemical gradient
The three ways that an ion channel can be gated include:
ligand-gated, voltage-gated, mechanically- (stress-) gated.
ligand-gated, ATP-gated, membrane-gated
temperature-gated, voltage-gated, NAD+ -gated
RNA-gated, diffusion-gated, osmotic pressure-gated
ligand-gated, voltage-gated, mechanically- (stress-) gated.
Which of the following channels would not be expected to generate a change in voltage by movement of its substrate across the membrane where it is found?
a sodium channel
a proton channel
a calcium channel
an aquaporin
an aquaporin
Which of the following statements about the ER network is NOT true?
The ER produces proteins that are sent to other organelles such as the Golgi, lysosomes, and the plasma membrane.
The ER is the most extensive membrane system in eukaryotic cells.
The ER is dynamic so tubules can be formed where needed.
The ER produces proteins that are sent out of the ER to many areas of the cytosol.
The ER produces proteins that are sent out of the ER to many areas of the cytosol.
Which of the following organelles is not part of the endomembrane system?
lysosomes
Golgi apparatus
the endosome
mitochondria
mitochondria
Mitochondria and chloroplasts are different from all other organelles in that they:
Use SNARE proteins to tether them to their proper locations in the cell
Possess their own small genomes and can make some of their own proteins
Are able to bud transport vesicles to remove toxic waste build-up
Have a symmetric single lipid bilayer surrounding them
Possess their own small genomes and can make some of their own proteins
ATP is important for chaperone protein function. Why would protein import into mitochondria be disrupted if ATP were depleted from inside mitochondria?
The protein would be blocked from entering the translocation apparatus
The translocation apparatus would be unable to function without ATP hydrolysis
The protein could slip back out of the mitochondria during transport
The signal sequence would not be recognized on the mitochondrial protein
The protein could slip back out of the mitochondria during transport
Proteins that are fully translated in the cytosol do not end up in
the interior of the nucleus.
transport vesicles.
the cytosol.
the mitochondria.
transport vesicles
Which of the following statements about vesicle budding from the Golgi is FALSE?
Adaptins interact with clathrin.
Clathrin molecules are important for binding to and selecting cargoes for transport.
Once vesicle budding occurs, clathrin molecules are released from the vesicle.
Clathrin molecules act at the cytosolic surface of the Golgi membrane.
Clathrin molecules are important for binding to and selecting cargoes for transport.
Which of the following statements about phagocytic cells in animals is FALSE?
Phagocytic cells extend pseudopods that surround the material to be ingested.
Phagocytic cells scavenge dead and damaged cells and cell debris.
Phagocytic cells are important in the gut to take up large particles of food.
Phagocytic cells can engulf invading microorganisms and deliver them to their lysosomes for destruction.
Phagocytic cells are important in the gut to take up large particles of food.
Which of the following choices reflects the appropriate order of locations through which a protein destined for the plasma membrane travels?
ER → Golgi → plasma membrane
lysosome → endosome → plasma membrane
Golgi → lysosome → plasma membrane
ER → lysosome → plasma membrane
ER → Golgi → plasma membrane
Which of the following is not unfolded during its import?
Proteins imported into the chloroplast
Proteins imported into the nucleus.
Proteins imported into the ER
Proteins imported into the mitochondria
Proteins imported into the nucleus.
v-SNARES participate directly in:
movement of the vesicle along cytoskeletal filaments
uncoating of the vesicle
docking of the vesicle to the target organelle
assembly or formation of the transport vesicle
docking of the vesicle to the target organelle
A key mechanism to bring a vesicle to a specific target membrane for fusion is:
Phosphorylation of t-SNAREs and v-SNAREs that unmask their binding domains that bring the vesicle close to the target membrane
Interaction of coiled coil domains on v-SNARES and t-SNARES that ratchet the two membranes, bringing them increasingly close until they fuse
Phospholipases on the naked transport vesicle will cleave the target membrane to allow fusion
Signal sequences on the clathrin coat are recognized by a docking protein on the target membrane
Interaction of coiled coil domains on v-SNARES and t-SNARES that ratchet the two membranes, bringing them increasingly close until they fuse
Which of the following statements is TRUE?
The signal sequences on mitochondrial proteins are usually at the C-terminus.
Most mitochondrial proteins are not imported from the cytosol but are synthesized inside the mitochondria.
Mitochondrial proteins cross the membrane in their native, folded state.
Chaperone proteins in the mitochondria facilitate the movement of proteins across the outer and inner mitochondrial membranes.
Chaperone proteins in the mitochondria facilitate the movement of proteins across the outer and inner mitochondrial membranes.
If you cloned a gene into a cell that encodes a protein with an ER signal sequence at its N-terminus and a nuclear localization sequence in its middle, where will the expressed protein be found?
in the nucleus
In the ER lumen
Half will be in the ER and half will be in the nucleus
It will be degraded in the lysosome
In the ER lumen
Which of the following statements about transport into mitochondria and chloroplasts is FALSE?
Proteins that are transported into these organelles are unfolded as they are being transported.
Signal peptidase will remove the signal sequence once the protein has been imported into these organelles.
After a protein moves through the protein translocator in the outer membrane of these organelles, the protein diffuses in the lumen until it encounters a protein translocator in the inner membrane.
The signal sequence on proteins destined for these organelles is recognized by a receptor protein in the outer membrane of these organelles.
After a protein moves through the protein translocator in the outer membrane of these organelles, the protein diffuses in the lumen until it encounters a protein translocator in the inner membrane.
All of the following targeting sequences are cleaved off during the import process EXCEPT:
The mitochondrial targeting sequence
The ER signal sequence
the nuclear localization sequence
The chloroplast targeting sequence
the nuclear localization sequence
Which of the following statements about nuclear transport is TRUE?
Nuclear import receptors bind to proteins in the cytosol and bring the proteins to the nuclear pores, where the proteins are released from the receptors into the pores for transit into the nucleus.
Nuclear pores are made up of many copies of a single protein.
Nuclear pores contain proteins with disordered segments that fill the channel and allow small water-soluble molecules to pass through in a non-selective fashion.
mRNAs and proteins transit the nucleus through different types of nuclear pores.
Nuclear pores contain proteins with disordered segments that fill the channel and allow small water-soluble molecules to pass through in a non-selective fashion.
Sorting information that directs trafficking or localization within the cell may be found on all of the following EXCEPT:
NLS
SNARE protein
chaperone
signal sequence
chaperone
Your friend works in a biotechnology company and has discovered a drug that blocks the ability of Ran to exchange GDP for GTP. What is the most likely effect of this drug on nuclear transport?
Nuclear transport receptors would be unable to bind cargo.
Nuclear transport receptors would be unable to enter the nucleus.
Nuclear transport receptors would be unable to release their cargo in the nucleus.
Nuclear transport receptors would interact irreversibly with the nuclear pore fibrils.
Nuclear transport receptors would be unable to release their cargo in the nucleus.
One of the three types of GTP-binding proteins, often called “G-proteins”, are membrane bound. These are the:
trimeric GTP-binding proteins
monomeric GTP-binding proteins
G-protein coupled receptors
Elongation factor GTP-binding proteins
trimeric GTP-binding proteins
What enzymatic activity does a G protein have?
GTPase activity
Phosphatase activity
Translocase activity
Kinase activity
GTPase activity
Which of the following is NOT true?
G proteins can hydrolyze GTP on their own but it is very slow
GDIs are necessary for G proteins to release GDP so they can bind GTP
G proteins can release GDP on their own but at an extremely slow rate
GAP proteins stimulate the rate of GTP hydrolysis by a G protein
GDIs are necessary for G proteins to release GDP so they can bind GTP
GTPase switch proteins such as ras:
Are converted from the active to inactive state by a guanine nucleotide exchange factor
are active when bound to GTP but inactive when bound to GDP
are active when bound to GDP but inactive when bound to GTP
synthesize GTP from GDP
are active when bound to GTP but inactive when bound to GDP
The Src homology 2 domain (SH2) binds:
cAMP
phosphorylated phosphinositol phospholipid
phosphotyrosine
proline-rich motif
phosphotyrosine