Membrane Structure (Module 2 Lecture 4) Flashcards
Name the two types of proteins in a plasma membrane as well as the modified carbohydrate motifs on the extracellular surface.
- Integral proteins (embedded in the membrane; usually a transmembrane) and peripheral proteins (which are loosely bound).
- Glycoproteins and glycolipids on extracellular surface
Describe two amphipathic lipids in a cellular membrane.
- Phospholycerides with varied polar head groups
2. Sphingolipids (including sphingomyelin and glycolipids)
Describe the asymmetry of plasma membranes.
- Outer leaflet contains more phosphatidylcholine and sphingomyelin as well as glycolipids.
- The inner leaflet contains more phosphatidylserine (charged) and phosphatidylethanolamine.
How do fatty acids module membrane packing?
- Cis-configuration unsaturated tails kink and cannot pack as closely as fully saturated tails.
- The more double bonds, the more fluid the membrane.
Describe the movement of phospholipids in the lipid bilayer.
- They can diffuse laterally in the membrane and can flex and rotate.
- They can move spontaneously from one side of the membrane to another but it is rare (flip-flopping).
- Flippases contribute to the synthesis of asymmetrical membranes.
Describe the role of cholesterol in plasma membranes.
It stiffens the region of the membrane adjacent to the steroid ring, strengthening the membrane while allowing the middle section of the bilayer to remain relatively fluid.
How are integral proteins removed from the plasma membrane?
They can only be removed using detergents because they are usually anchored from membrane leaflet to the other side and have hydrophilic portions on both sides.
How are peripheral proteins removed from the plasma membrane?
They are solubilized from the membrane by aqueous solvents like high salt buffers due to the fact that they are not fully embed in the membrane.
List four functions of integral proteins in plasma membranes.
- Transporters
- Anchors
- Receptors
- Enzymes
Describe the structure of a typical integral transmembrane protein.
- Contains alpha-helical structure made of non-polar amino acids.
- Contains oligosaccharide chains and disulfide bonds, all on the non-cytosolic surface of the membrane.
Can some transmembrane proteins pass through the membrane more than once?
Yes, and can have hydrophobic portions that are alpha-helices of beta-pleated sheets.
Describe the hormone receptors in plasma membranes linked to G proteins.
They have several spanning domains, like many other hormone receptors and include receptors for epinephrine and glucagon.
What is epinephrine?
Adrenaline (a hormone and neurotransmitter)
What is a G protein?
Guanosine-nucleotide binding proteins usually serve as switches in the cell membrane that can activate a cascade of subsequent reactions.
What is glucagon?
The hormone made in the pancease that breaks stored glygogen into glucose.