Unit 4 Flashcards
Membrane functions
- Compartmentalization (euks): create separate environments for different activities
- Selectively permeable barrier: prevent unrestricted molecule exchange
- Transport solutes: molecule exchange across membrane
- Energy transduction: convert from one form to another
- Respond to external signals: signals travelling from distance/nearby cells
- Scaffold for biochemical activities
What are membrane phospholipids composed of?
Polar head group, phosphate, glycerol, 2 fatty acid chains
Major polar head groups of phospholipids
Used for naming
- Phosphatidyl… choline (PC), serine (PS), ethanolamine (PE), inositol (PI)
Amphipathic
Have both hydrophilic and hydrophobic parts
e.g. phospholipid, cholesterol (sterol), glycolipid
Formation of lipid bilayers
- Hydrophobic molecules exclude water, clustering together to minimize energy cost of organizing water molecules
- Amphipathic molecules –> conflicting forces –> solved by formation of bilayer (energetically most favourable, spontaneous)
- Lipid bilayers are: closed, self-sealing
- Sealed compartment formed by phospholipid bilayer –> energetically favourable vs planar phospholipid bilayers (edges exposed to water)
Movement of phospholipids within membrane
- Phospholipids –> constantly moving within leaflet: lateral diffusion (swapping places within leaflet), twisting, turning, rotation
- Intentional movement: flipping to opposite leaflet during membrane synthesis (rarely flip back)
Allows membrane fluidity
Factors that affect membrane fluidity
- Temperature
- Change in lipid composition that affect alignment of phospholipid tails
Tightly packed tails –> more viscous, less fluid
Freely moving tails –> higher fluidity
Interaction between temperature + lipid composition
Membrane fluidity will change if:
- temp changes, lipid composition stays constant
- lipid composition changes, temp stays constant
Transition temperature (Tm)
Temp at which a membrane transitions b/w fluid phase + gel phase
If temp above Tm
Membrane ‘melts’ –> lipids move more freely, rotationally, laterally within leaflets
If temp below Tm
Hydrophobic tails pack together (as if cold, huddling together) –> membrane gels –> incompatible with life
Tm + membrane fluidity
Cells must maintain fluidity within a relatively narrow range even w/ changes in environmental temp
Usually deal with too cold temps
Factors that affect Tm (fatty acids)
- Altering length of fatty acid chains
- Longer chains –> more interactions b/w fatty acid tails –> tighter packing –> less fluid at a given temp, higher Tm, higher temp to melt - Altering saturation of fatty acids –> # of db
- More db (more unsat) –> less packing –> more fluid at given temp, lower Tm, lower temp to melt
- Membrane phospholipids typically have 1 sat fatty acid and 1 w/ 1+ db (unsat)
Factor that affects Tm (sterols)
- Altering amount of sterol (e.g. cholestrol) - (can be up to 50% of membrane lipid in animal cells)
- Cholesterol acts as “buffer”, inhibiting phase transitions when temp changes
- Higher cholesterol at cool temps –> more fluid
- Higher cholesterol at warm temps –> less fluid
Examples: variability of membrane fluidity between organisms (within life compatible range)
- Organisms from warm climates –> membranes near melt
- Organisms from cold climates –> membranes near gel
Mechanisms of membrane fluidity regulation in living cells
Homeo viscous adaptation (whole organism level): maintaining fluidity at temps low enough for potential gelling by altering membrane composition
Dealing with low temps:
- Shorter fatty acid chain length (e.g. enzymes cut C18 –> C16)
- Increase # db (= decrease sat): (e.g. desaturase enzymes triggered by low temps)
Membranes of archaea vs eubacteria + eukaryotic
Both: glycerol, phosphate, 2 HC chains
Archaea: branched ISOPRENE chains (instead of fatty acids) ETHER-linked to L-glycerol
- Allow extremophile archaebacteria to not suffer from membrane breakdown
Eubacteria/Euk: fatty acid chains ESTER-linked to D-glycerol
Ways proteins can associate w/ membranes
Integral:
- Transmembrane (across entire membrane, both leaflets, external parts outside membrane: alpha-helix, beta sheet
- Monolayer-associated: 1 leaflet
- Lipid-linked: linked to membrane by a lipid
Peripheral:
- Protein-linked: fully outside membrane, linked by integral protein
Integral protein association w/ membrane
- Hydrophobic R groups allow protein to be located in hydrophobic environment (hold orientation in membrane) since the backbone of protein is always hydrophilic (polar)
- Polypeptide chains usually cross membrane as alpha-helices
Formation of hydrophilic channels
- From several alpha-helices
- Hydrophobic parts hold protein in membrane
- Hydrophobic parts (very polar) form pore that water and small soluble molecules can flow through
Formation of Porins
- From beta pleated sheets
- Common in outer membranes of gram-negative bacteria + endosymbiont derived organelles
- Not common in animals
- Very common in bacteria
Movement restriction of membrane proteins
Restriction of movement by:
- Cytosolic protein
- Extracellular protein
- Identical/non-identical proteins of separate cells interact
- Large membrane protein prevents flow of membrane proteins (e.g. tight junction)
Membrane protein distribution in epithelium
- Tight junctions create 2 different domains in the membrane, prevent protein movement
- Epithelial cells: line tubular + spherical organs (can bring things in/move things out)
Apical domain
Domain on top section of cell
Basalateral domain
Domain on bottom and side (separated from apical domain)
Membrane glycoproteins
- Membrane proteins are coated with sugars on the extracellular side of the membrane
- “Glyco calyx” –> sugar coat(ed)
Preservation of membrane symmetry during transport process (sugars)
- Sugar added to protein in Golgi always on non-cytosolic side
- First in the Golgi lumen, then inside the vesicle, then the extracellular side of membrane
What is the most extensive membrane compartment?
The ER, especially rough ER
Where is new membrane added in a cell?
The ER