Chapter 11: Biological Membrane and Membrane Transport Flashcards
1
Q
- Which molecules make up nearly all the mass of biological membrane?
- Each membrane type has… what does this imply?
- How do these constituents vary?
- How does the inner face of the membrane differ from the outer face?
A
- Proteins, Polar Lipids, and Carbohydrates
- Characteristic lipids, implies that there is regulatory controls on:
- Lipid synthesis
- Lipid transport
- Membrane assembly
- Vary based on climate but not on diet. Diet determines what is available, not how it’s used.
- Differ based on the distribution of membrane lipids.
2
Q
- What is unique about membrane proteins?
- When does membrane protein composition change?
- In what ways do they associate with the membrane?
- How thick is the membrane?
- What is it permeable to?
- What do Glycerophospholipids, sphingolipids and sterols form?
- How do nonpolar and polar elements arrange themselves? What does this imply?
A
- Content in/on membrane varies widely (varies with cell type).
- Changes with conditions, such as diet.
- Associate with membrane:
- Span both layers
- Only on one face
- Loosely associated with one face
- 50-80 A (5-8 nm)
- Semi-permeable, permeable to nonpolar compounds.
- Form Liposomes (form a cell membrane).
- Non-polar elements face each other internally. Polar head groups face outward. Implies asymmetry.
3
Q
- What are the three biological membrane lipids?
- What makes these lipids unique?
- How do they form?
- Micelle: What are their organization?
- How do they form?
A
- Glycerophospholipids, Sphingolipids, and Sterols
- All are virtually insoluble in water.
- Form spontaneously, the goal is to minimize contact with water. So, hydrophobic interactions drive the formation of the membrane.
- Spherical, hydrophobic, acyl chains inside. Polar head groups outside.
- Form easily from free fatty acids, lysophospholipids, and detergents.
4
Q
- Bilayer: How are lipids arranged?
- What do they form from?
- Liposome: How is the structure arranged?
- What make the liposome special?
A
- Lipids are arranged as a sheet.
- Acyl chains apposed.
- Head groups outside and inside
- Bad because hydrophobic sides are exposed.
- Forms from glycerophospholipids and sphingolipids.
- A vesicle (sphere)
- Head groups in the center and on the outside.
- Inner head groups form a second, isolated aqueous environment.
- Closed surface that can interact all the way around when in aqueous solution.
5
Q
- What does the degree of mobility of lipid in the membrane depend on?
- If lipid composition does not change, then what happens?
- At low temperatures?
- At high temperatures?
- At intermediate temperatures?
- What is phase change defined as?
- What lowers the transition temperature?
- What do sterols do ?
A
- Depends on temperature and lipid composition.
- No change in lipid composition:
- Lipids solidify into a Paracrystal
- Lipids in a fluid state (liquid disordered)
- Gel in most membranes (liquid ordered)
- Phase Change: defined as transition temperature
- The more unsaturated fatty acids = lower transition temperature.
- Sterols change transition temperature,
- Adjust ordering of acyl chains.
- Promote liquid-ordered state.
6
Q
Three levels of membrane mobility
- What is first level?
- What is second level?
- What is catalyzed movement?
- What does Flipases do?
- What does Floppases do?
- What do Scamblase do?
A
- Lipids move very slowly from one leaflet to the other (A).
- Lipid acyl chains move freely and rapidly through the plane of the membrane (B).
- Catalyzed movement from one side of bilayer to the other (C).
- Moves lipid from outer to cytosolic leaflet via ATPases.
- Moves lipid from cytosolic to outer leaflet via ATPases.
- Scamblase moves lipids in either direction toward equilibrium.
7
Q
- Peripheral Proteins:
- How are they associated with the membrane?
- What are they regulators of?
- Integral Proteins:
- What are they anchored to?
- How are they removed?
- What are transmembrane proteins?
- How are they oriented?
- Where is carbohydrate located?
- Type I-V?
- Type V
- Type VI
- What is an example of Peripheral Proteins?
- How does it function?
- Where is it found?
- What is its function?
A
- Peripheral Proteins:
- Via H-bonds and electrostatic interactions with integral proteins, or polar head groups of lipids.
- Limit integral protein mobility.
- Integral Proteins:
- Firmly anchored to the membrane
- Removed by detergents or organic reagents. Must disrupt the membrane bilayer and hydrophobic interactions.
- A subclass of integral proteins. Span the lipid bilayer. Usually asymmetric and most have polar and nonpolar regions.
- Oriented asymmetrically within the membrane. Amino terminus: Outside, Carboxy terminus: Inside
- Carbohydrate is always on the outside of the plasma membrane.
- Type I: One polypeptide, Amine group outside. Type II: One polypeptide, Amine group inside. BOTH have one transmembrane domains. Type III and IV BOTH have multiple transmembrane domains.
- Type V: One acyl anchor, Peripheral, Inside
- Type VI: Two acyl anchors, Integral, Outside
- Annexin Family would be an example of Peripheral Proteins
- Binds acidic membrane phospholipids in a Ca2+ dependent manner.
- Found on the inner surface of the plasma membrane, outer surfaces of intracellular vesicles.
8
Q
- Some peripheral proteins have covalently attached….?
- What Type is this?
- What does this provide?
- Where are they founds?
- What Type is Glycosylated Phosphatidylinositols (GPI)?
- Describe GPI
A
- Lipids
- Type V membrane protein.
- Provides a weak membrane anchor
- Found on the inner surface of the plasma membrane.
- Type VI, found on the outer surface.
- Not released by alkali, integral by definition, only on extracellular face.
9
Q
- What is an Integrin?
- What type are they?
- What do they bind?
- What are Cadherins and Selectins?
- What are all these proteins involved in?
A
- Involved in cell signaling, adhesion, and cell-cell interactions. Heterodimeric: 14 alphas, 8 beta.
- Type IV membrane protein
- Extracellular domain binds specific extracellular ligands. Many possible alpha/beta combinations mean many potential ligand binding sites.
- Cadherins, Immunoglobulin-like proteins and Selectins function alike.
- Adhesion
10
Q
- What are Microdomains (Rafts)?
- What do they contain?
- What is the combind function of these proteins?
- What are caveolae?
- What do they span?
- What are they bounds to?
- What do they function in?
A
- Thicker regions of the membrane enriched in certain proteins and lipids.
- Contain Sphingolipids, Cholesterol, Lipid-linked proteins with 2 palmitoyl or myristoyl groups, and GPI-linked proteins.
- Function as a unit to change membrane shape.
- Curved areads of the membrane.
- Span both leaflets.
- Caveolin in high concentration, bound to 3 fatty acyl chains per molecule.
- Functions in endocytosis.
11
Q
- What does Membrane Fusion allow?
- What do Membrane Channels allow?
- What does Passive Transport facilitated by?
- What is Simple Diffusion?
- What is Membrane Potential?
- What do both Simple Diffusion and Membrane Potential define?
- What does a selectively permeable membrane plus an unequal distribution of charged solute result in?
A
- Membrane Fusion allows larger things in and out.
- Membrane Channels allow smaller things in and out.
- Membrane Proteins
- Two compartments, Unequal solute concentrations, Separation of compartments by permeable barrier.
- Movement of particles until an equilibrium is achieved. Conc 1 = Conc 2
- An electrical gradient caused by an unequal charge distribution. Charged particles move until they achieve charge equilibrium.
- Define Biomembrane Electrochemical Gradient
- Results in unequal solute concentration and charge concentration between both sides of the membrane.
12
Q
Solute Transport
- What must a solute do to get through a membrane?
- What are the three classes of membrane transport systems?
- What are two fundamental mechanisms for transportation?
- What is passive transport?
- What proteins assist in passive transport?
- Give an example
A
- Strip away solvation layer, move past hydrophobic molecules and re-solvate.
- Physical barrier must be overcome with energy.
- So much energy that membranes are virtually impenetrable to polar solutes.
- Uniport, Symport, Antiport.
- Passive and Active Transport
- Passage of polar solutes made thermodynamically favorable. Membrane proteins decrease required activation energy. Passive cannot go against the gradient.
- Transporters or Permeases
- Span the membrane, often multiple times.
- Bind with specificity and stereo-specificity
- Bind using weak interactions.
- Glucose Transporter: Polar groups in the middle of the membrane so they can interact with the glucose to help transport it across the cellular membrane. H-bonds helps with this transport.
13
Q
Passive (Facilitated Diffusion)
- Give an examle
- How does this mechanism work?
A
- Erythrocyte Anion Exchanger
- Co-Transport, an example of an antiport. Cl- moves into the cell while HCO3- moves out of the cell (respiring tissues). Or vice-versa (lungs). Does not change Vm.
14
Q
- What is Active Transport?
- When is it thermodynamically favored?
- What does the picture show?
- What does the movement of ions create?
- What transport is this?
A
- Movement against the electrochemical gradient.
- Thermodynamically favored only when it’s coupled an exergonic process (Absorption of light, Oxidation reaction, Breakdown of ATP)
- Primary active transport creates an electrochemical gradient which facilitates the movement of S2 through the secondary active transport, against its gradient.
- Movement creates an electrical potential (Eukaryotic membranes have a potential of 0.05-2.0 V)
- This is electrogenic transport
15
Q
- What are Ion-selective channels?
- What are they coupled to?
- How are they different from Ion transporters?
- What is Ligand Gated?
- What is an example?
- What is Voltage Gated?
- What is an example?
A
- Move certain ions only.
- Often coupled to rapid changes in membrane electrical potentials.
- Move several orders of magnitude more molecules.
- Do not become saturated (rates are not maximal at very high substrate.
- Open and close in response to a cellular event.
- Binding of molecules induces the opening of the channel.
- Acetylcholine Receptor: Bind is cooperative, allosteric effect causes twisting.
- Twisting is conformation changes and changes in weak interactions.
- Channels open
- Ion movement is very fast.
- Acetylcholine Receptor: Bind is cooperative, allosteric effect causes twisting.
- Protein conformation changes in respones to a threshold membrane potential that was achieved.