Membrane Composition Flashcards

0
Q

What is the composition of phospholipids?

A

Glycerol bound to fatty acid chains (ester bonds) and to a head group by a phosphate molecule

Head group determines type of phospholipid e.g. choline, inositol, amines, sugar

note: cis double bond in fatty acid chain introduces kink - reduces phospholipid packing

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1
Q

List some general and specific functions of biological membranes.

A

GENERAL:

  • continuous, highly selective permeable barrier
  • control of enclosed chemical environment
  • communication
  • recognition of signalling molecules, adhesion proteins, and immune surveillance
  • signal generation in response to stimuli

SPECIFIC:

  • interaction with adjacent cells
  • absorption & secretion
  • changing shape for transport
  • synapses: electrical signal conduction
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2
Q

What is the composition of sphingomyelin?

A

Phosphocholine bound to fatty acid (but NO GLYCEROL)

Often found in myelin sheaths

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3
Q

What is the composition of a glycolipid, and what two types are there?

A

Replace sphingomyelin phosphocholine with sugar

CEREBROSIDE = sugar monomer head group

GANGLIOSIDE = oligosaccharide head group

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4
Q

Describe the range of motion of phospholipids.

A

LATERAL DIFFUSION

ROTATION

FLEXION (vibration)

FLIP-FLOP (rare - high energy conformation needed)

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5
Q

Describe how cholesterol affects phospholipid packing.

A

OH forms hydrogen bonds with fatty acids -> reduced phospholipid chain motion -> reduced fluidity

Forces phospholipid molecules further apart -> reduces phospholipid packing -> increased fluidity

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6
Q

How does cholesterol make membranes more stable?

A

Eliminates endothermic phase transition of phospholipid bilayers, therefore less energy required to be fluid.

note: formation of crystalline islands -> fractures -> leakage

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7
Q

Describe the range of motion of proteins in phospholipid bilayers.

A

LATERAL DIFFUSION
CONFORMATIONAL CHANGE
ROTATION

note: NO FLIP-FLOP (proteins too large/hydrophobic)

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8
Q

What is the evidence that there are proteins in membranes (generally)?

A

Functional:

  • facilitated diffusion
  • ion gradients
  • specificity of cell responses

Biochemical:

  • membrane fractionation
  • freeze fracture
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9
Q

How is the movement of membrane proteins restricted?

A

Aggregation of adjacent membrane proteins

Tethering of membrane proteins (intracellularly or extracellularly)

Interaction with membrane proteins of other cells

How fluid the surrounding lipid parts of the membrane are

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10
Q

What is the functional difference between integral and peripheral membrane proteins, and how can they each be separated from the membrane?

A

INTEGRAL:
Interact with hydrophobic domains of lipid bilayer.
Only removed with agents that compete for these interactions e.g. detergents, organic solvents

PERIPHERAL:
Form electrostatic interactions/hydrogen bonds with phosphate heads
Removed by changes in pH/ionic strength

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11
Q

Describe the components of the cytoskeleton.

A

Spectrin (alpha and beta subunits in antiparallel arrangement)

Ankyrin between membrane proteins and spectrin

Actin cross links & adducin present

Band 3, glycophorin (band 7) in membrane; band 4.1 by actin

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12
Q

What two disorders can result from reduction/defect of spectrin?

A

Hereditary spherocytosis:

  • spectrin depleted by ~40%-50%
  • erythrocytes round up
  • less resistant to lysis - cleared by spleen (anaemia)

Hereditary elliptocytosis:

  • defect in spectrin molecule - unable to form heterotetramers
  • fragile elliptoid cells
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13
Q

How might a membrane protein interact with the hydrophobic domain of the membrane bilayer?

A
  • transmembrane sequence: ~20-22aa with hydrophobic R regions
  • lipid-linked proteins: insertion of hydrophobic lipid moieties e.g. palmitoylation, mystriolation
  • insertion of amphipathic alpha-helix from cytoplasmic side
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