Week 1 - Biological membranes Flashcards

1
Q

What are the main functions of a biological membrane?

A
  • Continuous, highly selective permeability barrier
  • Allows control of the enclosed chemical environment
  • Communication (can control the flow of information between cells and their environment)
  • Recognition (signalling molecules, adhesion proteins, immune surveillance)
  • Signal generation in response to stimuli (electrical or chemical)
    Different membranes have specialised functions too
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2
Q

Describe the composition of biological membranes

A

Varies depending on source
Dry weight : approx. 40% lipid, 60% protein and 1-10% carbohydrate
20% of the total membrane weight is water

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3
Q

What are the modes of mobility for lipid molecules in a lipid bilayer?

A
  • Intra-chain rotation: kink formation of the fatty acyl chain
  • Fast-axial rotation
  • Fast-lateral diffusion within the plane of the bilayer
  • Flip-flop: movement of lipid molecules from 1 half of the bilayer to the other on a 1-for-1 exchange basis
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4
Q

How can unsaturated hydrocarbon chains affect fluidity?

A

If they have cis double bonds, they can disrupt phospholipid packing, which helps to maintain fluidity

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5
Q

What are the main types of lipids?

A
  • Membrane lipids (amphipathic molecules)
  • Phospholipids (head group and fatty acid chain)
  • Sphingomyelin (only phospholipid not based on glycerol)
  • Predominant lipids
  • Glycolipids
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6
Q

What are the different types of glycolipids?

A
  • Cerebroside: only has a single sugar monomer head group

- Ganglioside: has complex carbohydrate head groups

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7
Q

Describe lipid bilayer formation

A
  • Amphipathic molecules form 1 of 2 structures in water (micelles and bilayers)
  • Bilayers are the favoured structure for phospholipids and glycolipids in aqueous media
  • Bilayer formation is spontaneous in water
  • Formation is driven by van der Waals
  • The structure is stabilised by non-covalent forces
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8
Q

What is the permeability of the lipid bilayer?

A

It has a very low permeability to ions and most polar molecules

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9
Q

What is the effect of cholesterol on membrane stability?

A
  • Can reduce the fluidity since it attaches itself, a rigid molecule, to a phospholipid hence reducing movement
  • Can increase the fluidity by affecting the phospholipid packing
  • At higher temperatures, cholesterol decreases membrane fluidity; at lower temperatures it increases membrane fluidity.
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10
Q

Describe the structure of cholesterol

A
  • Polar head group
  • Rigid planar steroid ring structure
  • Non-polar hydrocarbon tail
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11
Q

How can membrane proteins associate with the lipid bilayer?

A

Peripheral =
- bound to surface
- electrostatic and hydrogen bond interactions
- removed by changes in pH or in ionic strength
Integral =
- interact extensively with hydrophobic domains of the lipid bilayer
- cannot be removed by manipulation of pH and ionic strength
- are removed by agents that compete for non-polar interactions

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12
Q

What evidence is there for membrane proteins?

A
Functional:
- Facilitated diffusion
- Ion gradients
- Specificity of cell responses
Biochemical:
- Membrane fractionation and gel electrophoresis
- Freeze fracture
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13
Q

How can membrane proteins move?

A
  • Conformational change
  • Rotational
  • Lateral
  • NO FLIP-FLOP
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14
Q

How can membrane protein mobility be restricted?

A
  • Aggregates
  • Tethering (to membrane or to cytoskeleton)
  • Interaction with other cells
  • Lipid mediated effects
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15
Q

How do membrane proteins contribute to the erythrocyte cytoskeleton?

A
  • The peripheral membrane proteins compose a membrane skeleton on the cytoplasmic face of the membrane
  • This cytoskeleton holds the shape of the RBCs
  • Composed of the protein spectrum and actin molecules
  • This actin-spectrin network is attached to the membrane by adaptor molecules (ankyrin and glycophorin)
  • Attachment of integral membrane proteins to the cytoskeleton restricts material mobility of the membrane protein
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16
Q

How are integral membrane proteins inserted into membranes?

A
  • They are synthesised against the mRNA template by ribosomes
  • The signal sequence at the N-terminus is recognised by a signal recognition particle (SRP)
  • Binding of the SRP to the growing polypeptide chain and the ribosome locks the ribosome complex and prevents protein synthesis while the ribosome is in the cytoplasm
  • On the ER, the SRP is recognised by a SRP receptor
  • In making the intersection with the SRP receptor, the SRP is released from the signal sequence
  • Further synthesis is directed into the lumen of the ER, as the ribosome is anchored to a pore complex
  • The protein contains a ‘stop transfer signal’, which is highly hydrophobic
  • It forms the transmembranous region of the protein and causes the rest of the protein to be translated in the cytoplasm
  • A lateral gating mechanism releases the membrane protein from the protein translator into the lipid bilayer
  • The ribosome detaches
  • Signal sequence is cleaved by signal peptidases
    Hence, a transmembrane protein with its N-terminus directed into the lumen and its C-terminus directed into the cytoplasm is produced.
17
Q

What is hereditary spherocytosis?

A

A haemolytic anaemia

  • Spectrin is depleted by 40-50%
  • Erythrocytes round up
  • Less resistant to lysis
  • Cleared by spleen
18
Q

What is hereditary elliptocytosis?

A

A haemolytic anaemia

  • Defect in spectrin molecules
  • Unable to form heterotetramers
  • Fragile elliptoid cells
19
Q

What are some properties of transmembrane domains?

A
  • Usually 18-22 amino acids long
  • The amino acids have hydrophobic R-groups
  • Have an alpha-helix usually