1.3 (Membrane Structure) Flashcards
Phospholipid molecules.
Have a polar (charged, hydrophilic) phosphate head and long non-polar (hydrophobic) lipid tails
Phospholipids emergent property.
Will self-organise to keep their heads ‘wet’ and their tails ‘dry’
What are integral proteins?
Integral proteins are permanently embedded, many go all the way through and are polytopic (poly = many, topic = surface), integral proteins penetrating just one surface are monotopic.
What are peripheral proteins?
Usually have a temporary association with the membrane, they can be monotopic or attach to the surface
What are glycoproteins?
- Proteins with an oligosaccaride (oligo = few, saccharide = sugar) chain attached.
- Important for cell recognition by the immune system and as hormone receptors
TRACIE.
- Transport: Protein channels (facilitated) and protein pumps (active)
- Receptors: Peptide-based hormones (insulin, glucagon, etc.)
- Anchorage: Cytoskeleton attachments and extracellular matrix
- Cell recognition: MHC proteins and antigens
- Intercellular joinings: Tight junctions and plasmodesmata
- Enzymatic activity: Metabolic pathways (e.g. electron transport chain)
What is cholesterol?
Makes phospholipids pack more tightly and regulates the fluidity and flexibility of the membrane.
Explain membrane fluidity.
- Hydrophobic hydrocarbon tails usually behave as a liquid. Hydrophilic phosphate heads act more like a solid.
- Difficult to determine whether the membrane is truly either a solid or liquid it can definitely be said to be fluid
Why is it important to regulate the degree of fluidity?
- Need to be fluid enough that the cell can move
- Need to be fluid enough that the required substances can move across the membrane
- If too fluid membrane could not effectively restrict the movement of substances across itself
Outline cholesterol’s role in fluidity.
- Presence of cholesterol in the membrane restricts movement of phospholipids and other molecules – reduces membrane fluidity
- Presence of cholesterol disrupts regular packing of hydrocarbon tails of phospholipid molecules - increases flexibility as it prevents tails from crystallising and behaving like a solid
- Reduces permeability to hydrophilic molecules and ions such as sodium and hydrogen
Evidence for fluid mosaic model.
Biochemical techniques:
- Membrane proteins found to be very varied in size and globular in shape
- Such proteins would be unable to form continuous layers on the periphery of the membrane
- Membrane proteins had hydrophobic regions and therefore would embed in the membrane not layer the outside
Fluorescent antiobody tagging:
- red or green fluorescent markers attached to antibodies which would bind to membrane proteins
- Red or green fluorescent markers attached to antibodies which would bind to membrane proteins
- Membrane proteins of some cells were tagged with red markers and other cells with green markers
- Cells were fused
- Within 40 minutes the red and green markers were mixed throughout the membrane of the fused cell
- Showed membrane proteins are free to move within the membrane, not fixed in a peripheral layer
Davson- Danielli model evidence.
Evidence:
- In high magnification electron micrographs membranes appeared as two dark parallel lines with a lighter coloured region in between
- Proteins appear dark in electron micrographs and phospholipids appear light - possibly indicating proteins layers either side of a phospholipid core
Model:
- Protein-lipid sandwich
- Lipid bilayer composed of phospholipids (hydrophobic tails inside, hydrophilic heads outside)
- Proteins coat outer surface
- Proteins do not permeate the lipid bilayer
Explains:
Despite being very thin membranes are an effective barrier to the movement of certain substances
Falsification of Davson-Danielli model.
Interpreting image:
- Fracture occurs along lines of weakness, including the centre of membranes
- Fracture reveals an irregular rough surface inside the phospholipid bilayer
- Globular structures were interpreted as trans-membrane proteins
Conclusion:
Contradicts Davson-Danielli model which only involves proteins coating the surface of the membrane