Cell Molecular Exam 3 Flashcards

(35 cards)

1
Q

Compare and contrast each of the following. Give an example of each.
a. Channels, transporters, and ATP-powered pumps

A

Channel - No energy, gated
(facilitated transport, specific protein)

Transporters - protein-lined pathway, hydrophobic barrier
(specific protein, Solute transported against its gradient, Driven by movement of a cotransported ion down its gradient)

ATP-powered pumps - hydrolyzed to bring molecules against concentration gradient
(Requires specific protein, Solute transported against its gradient, Coupled to ATP hydrolysis)

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2
Q

Compare and contrast each of the following. Give an example of each.
b. Uniporters, symporters, and antiporters

A

Uniporters - transports glucose and amino acids across cellular membrane (facilitated transport)

Symporters - Glucose and amino acid against high concentration gradient. (Cotransport, solute against concentration gradient, driven by movement of cotransport ion)
Transport in the same direction

Antipoter - Transports various ions and sucrose
(Cotransport, solute against concentration gradient, driven by movement of cotransport ion)
Transport in opposite direction

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3
Q

Compare and contrast each of the following. Give an example of each.
c. Simple diffusion, facilitated transport, cotransport, and active transport

A

Simple diffusion - O2, CO2, steroid hormones, many drugs
(requires no energy)

Facilitated transport - Uniporters and Channels
(Requires specific protein)

Cotransport - uses the energy released by ion (H+/ Na+) movement down its electrochemical gradient
(Requires specific protein, solute against concentration gradient, driven by movement of cotransport ion

Active transport - ATP-powered pumps (Requires specific protein, Solute transported against its gradient, Coupled to ATP hydrolysis)

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4
Q

Describe the structure and function of each of the following.
a. GLUT1

A

Function: uniporter transports glucose across cellular membranes.

Structure: Hydrophobic central cavity. Two conformation outside open vs inside open.

The cycle
1) Outward open
2) Ligand-bound occluded
3) Inward open
4) Ligand-free occluded

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5
Q

Describe the structure and function of each of the following.
b. Na+/K+ ATPase

A

P-class pump (1 atp hydrolysis domain)

antiporter (pumps in opposite directions)

Inward binds three Na and outward binds two K. (binding site for 5 ions)

The cycle
Moves three Na+ ions out of and two K+ ions into the cell per ATP molecule hydrolyzed

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6
Q

Describe the structure and function of each of the following.
c. CFTR

A

Function: Transports Cl ions

Structure: Dephosphorylated closed, phosphorylated R domain removed, ATP-bound open
2 Subunits (channel with use of ATP, doesn’t pump ions but opens and closes using ATP)

ABC class protien

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7
Q

Describe the structure and function of each of the following.
d. K+ channel

A

Structure: pore helix, selectivity filter. Amino acids around are just the right size/interactions

simple channel no ATP hydrolysis

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8
Q

Describe the structure and function of each of the following.
e. Na+/galactose symporter

A

Na+-linked symporters enable animal cells to import glucose and amino acids against high concentration gradients.

Na+ linked to galactose

Sodium down gradient, galactose against
Multiple transmembrane helix’s
Binding sites for Na and galactose
Symporter – driven by sodium down gradient
Opens one side to bind both together
Outside open vs inside open

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9
Q

How is the resting membrane potential maintained in an animal cell?

A

Generated by the ATP-powered Na+/K+ pump and nongated K+ channels.

(Channels and proteins)

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10
Q

How does the electrochemical gradient across a cell membrane determine the direction of ion movement across the membrane? What two forces are acting on the ions?

A

Ion concentration gradient

Membrane electric potential

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11
Q

How is pH maintained in the cytoplasm and organelles of eukaryotic cells?

A

Proton pumps that pump hydrogen
V-class pumps (hydrolysis ATP to pump protons into vacule to acidicize it)

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12
Q

How are molecules transported across intestinal epithelial cells from the intestinal lumen to the blood? Which transporters in the apical and basolateral membranes are involved?

A

Carbon dioxide transport in blood requires a Cl−/HCO3− antiporter.

Needs three channels: one across the apical membrane, the basolateral, and one that pumps sodium.

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13
Q

Define each of the following:
a. Chemiosmosis

A

The interconversion of three forms of biological potential energy: chemical bond energy, chemical gradients across membranes, and electrical gradients across membranes.

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14
Q

Define each of the following:
b. Proton-motive force

A

Energy is stored in proton electrochemical gradient and used in ATP synthesis.

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15
Q

Define each of the following:
c. Electron carrier

A

H2O to O2

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16
Q

Define each of the following:
d. Aerobic oxidation

A

Cells use a four-stage process to convert energy released from glucose/fatty acid oxidation into ATP phosphoanhydride bond.

17
Q

Compare and contrast aerobic oxidation and photosynthesis. In which organelle does each take place? What is the energy source? What are the end products?

A

Aerobic Oxidation - Mitochondria use AO of carbon containing molecules to generate ATP.

Photosynthesis - Chloroplasts; Plant photosynthesis principal end products are O2 and polymers of 6-carbon sugars (starch and sucrose).
Light-capturing and ATP-generating photosynthesis reactions occur in chloroplast thylakoid membranes.

Each - have their own DNA, ATP production

18
Q

What are the 4 stages of aerobic oxidation? Where does each step take place?

A

1) GLYCOLYSIS - Cytosolic enzymes convert glucose to 2 molecules of pyruvate and generate 2 molecules each of NADH and ATP.
2) CYTRIC ACID CYCLE - the 3-carbon pyruvate molecule is oxidized to generate one molecule each of CO2, NADH, and acetyl CoA, which is oxidized to CO2 by the citric acid cycle
3) ELECTRON-TRANSPORT CHAIN - flow of electrons from NADH/FADH2 through the electron transport chain complexes provides energy to drive H+ transport across the inner mitochondrial membrane, generating a proton-motive force (voltage and pH gradients).
4) CALVIN CYCLE - Reduction potentials of the electron carriers favor unidirectional, “downhill,” electron flow from NADH and FADH2 to O2 to form H2O.

19
Q

What are the 4 stages of photosynthesis? Where does each step take place?

A

1) light absorption, generation of high-energy electrons, and O2 formation from H2O (Thylokoid)
2) Electron transport leading to reduction of NADP+ to NADPH and PMF generation (Thylokoid)
3) ATP synthesis (Thylokoid)
4) conversion of CO2 into carbohydrates (carbon fixation) (Stroma)

20
Q

What is the energy yield of glycolysis? Is it aerobic or anaerobic? How is the rate of glycolysis regulated? What are the possible fates of pyruvate?

A

2 molecules of pyruvate and generate 2 molecules each of NADH and ATP.

Anaerobic process

Metabolize pyruvate to lactic acid or ethanol and CO2 to convert NADH back to NAD+ required for glycolysis

21
Q

What is the energy yield of the citric acid cycle? Is it aerobic or anaerobic?

A

3-carbon pyruvate molecule is oxidized to generate one molecule each of CO2, NADH, and acetyl CoA, which is oxidized to CO2 by the citric acid cycle

aerobic

22
Q

What is the function of each of the following?
a. NADH and FADH2

A

Provides energy to drive H+ transport across inner mitochondrial membrane.

23
Q

What is the function of each of the following?
b. Acetyl-CoA

A

The end product of fatty acid oxidation and glycolysis. Important intermediate in the aerobic oxidation of pyruvate, fatty acids, and many amino acids

Contributes acetyl groups to many biosynthetic pathways

24
Q

What drives progression through the electron transport chain?

A

proton-motive force

Reduction potentials of the electron carriers favor unidirectional, “downhill,” electron flow from NADH and FADH2 to O2 to form H2O.

25
What enzyme makes ATP? Describe the mechanism of the enzyme.
ATP synthase. F0 and F1. Rotates as protons pass through, which combines to ATP/ADP. Switching between the two-conformation making ATP. Protons passing through cause rotation, which causes subunits to switch conformation. 3 ATP per rotation.
26
What is the difference between C3 and C4 plants?
C3 plants, a substantial fraction of the CO2 fixed by the Calvin cycle can be lost during photorespiration, which is favored at low CO2 and high O2 levels. C4 plants fix CO2 in outer mesophyll cells into 4-carbon molecules that are shuttled to the interior bundle sheath cells for use in the Calvin cycle, decreasing the loss in respiration.
27
Are proteins transported to the ER during or after translation? What is the role of the signal sequence, SRP, and translocon?
SRP binds to the receptor. A signal sequence, SRP, and SRP receptor system docks the ribosome on an ER translocon and cotranslationally inserts the nascent protein into or through the ER membrane.
28
How is membrane protein topology predicted based on the amino acid sequence?
Has STA (stop transfer sequence, type 1) and SA (internal signal sequence) Hydropathy profile - Anything above 0 is hydrophobic (in membrane) - How many transmembrane membranes (anything over 1 is type 4) - Cant identify between type 1 and 3 (would need to know charges)
29
What are the 6 classes of ER membrane proteins? How is each inserted into the membrane?
Type I - Single-pass transmembrane proteins, signal sequence cleaved, brought to Er, stop transfer sequence. N in lumen and C in cytosol. Type II - no cleaved signal sequence. N in cytosol and C in lumen Type III - no cleaved signal sequence. C in cytosol and N in lumen Tail-anchored protein - N in cytosol Type IV - multiple subclasses, similar to type II/III, 4A/4B, N-terminus cytpoplasimic/lumen. + change N-terminus stays lumen, + charge C-terminus translocated to Lumen. GPI-anchored protein - no transmembrane domain, lipid anchored, enzyme cut sequence. Protien transferred to membrane. N in lumen
30
What is the role of each of the following: a. Protein Disulfide Isomerase (PDI)
Forms correct disulfide bonds. CYS held by sulfide bond, helps create disulfide bonds
31
What is the role of each of the following: b. Peptidyl-Prolyl Isomerase (PPI)
Helps proline residues fold correctly.
32
What is the role of each of the following: c. N-linked oligosaccharides
Used to monitor folding and for quality control * Modification in ER, glycoxidation adding saccharides to protein * Added in ER while protein translated * Added to nitrogen * Precursor assembled (n-acetylglucosamine, mannose, glucose) attached to protein (ASN). Function: Folding, stability, adhesion, and recognition
33
How does targeting to the mitochondria, chloroplasts, and nucleus differ from targeting to the ER?
ER - Signal N-terminus (Location of Sequence Within Protein), will be cleaved. Core of 6-12 hydrophobic amino acids Mitochondria - Longer signal sequence, N-terminus (Location of Sequence Within Protein), will be cleaved. Amphipathic helix. Chloroplasts - Signal N-terminus (Location of Sequence Within Protein), will be cleaved. No common motifs. Nucleus - Signal varies (Location of Sequence Within Protein). Will not be cleaved. Multiple different kinds.
34
Describe the structure and function of the nuclear pore complex (NPC).
Pore structure made of Y complexes that make ring Net of proteins (nuclear porins) FG-nucleoporin mesh, keeps anything without signal out Direct protiens to the nucleus.
35
What processing does a protein undergo in the ER?
modifications, folding, quality control