Membranes Flashcards
What is the major component of membranes and what is there structure?
Phospholipids (amphipathic) -
Hydrophillic phosphate group
Glycerol
2 hydrophobic fatty acid tails
What is a glycolipid and what are the 2 examples?
Phospholipids whose phosphate group has been replaced by a sugar group
Cerebrosides: monosaccharide group
Ganglioside: Oligosaccaharide group
Define mobility
Define fluidity
Ability of a single phospholipid to move
Ability of the membrane to move
What kind of mobility do phospholipids have?
Flexion (lowest energy)
Rotation
Lateral diffusion
Flip-flop (highest energy)
Describe the features of the two types of fatty acid tails
Saturated:
Only C-C bonds (no kinks)
Increased packing and decreased fluidity
Unsaturated:
Some C=C double bonds (cis-kinked)
Increased fluidity and decreased packing
Describe the structure of cholesterol and their specific functions
Very small Hydrophillic OH group: forms H-bonds with C=O on fatty acids
Rigid planar steroid ring: restricts movement
Flexible Hydrophobic hydrocarbon chain: allows movement
What is the function of cholesterol in the membrane?
Prevents membrane becoming semi-crystalline
Keeps the membrane at constant fluidity:
High temperatures - restricts movement
Low temperatures - restricts packing
What are the two types of membrane proteins and how are they bonded to the membrane?
Peripheral (hydrophillic) - forms van der waals forces and H-bonds with phosphate groups
Integral (hydrophobic) - bound to the middle of the membrane by the hydrophobic effect
How can membrane proteins be removed from the membrane?
Peripheral - changes in pH, ionic concentrations
Integral - other non-polar organic solvents
What kind of mobility do membrane proteins have?
Flexion
Rotation
Lateral diffusion
(No flip-flop)
What restrictions do membrane proteins have on their mobility?
Proteins separate out in the bilayer
Associations with extramembrous proteins and other membrane proteins
What is the structure of the erythrocytes cytoskeleton?
Forms a membrane skeleton:
Protein spectrin is a heterotetramer of alpha and beta chains which attaches to the membrane to produce the biconcave shape
Ankyrin (band 4.9) and band 4.1 attach spectrin to the glycoproteins band 3 and glycophorin A respectively
What are to haemolytic anaemias caused by defective spectrin?
Spherocytosis:
Lack of spectrin, erythrocytes round up and lyse
Elliptocytosis: Abnormal spectrin (cannot form heterotetramers)
How are proteins destined for secretion transported to the ER?
SRP (Signal recognition particle) binds to partially synthesised protein (at the signal peptide sequence) and transports it to a translocation channel
Protein is released from the ribosome into the ER lumen
Signal peptide sequence is cleaved by signal peptidase
How are Membrane proteins transported into the ER and how is orientation determined?
Contain a stop transfer sequence (hydrophobic region of the peptide) that prevents full translocation of the protein
Depending on the location of the charges on the protein and whether or not it is cleaved will determine the orientation of the protein