Session 1 - Lipids, Proteins + Membrane Structure Flashcards

(29 cards)

1
Q

What is the composition of the dry weight of the membrane?

A
  • 40% Lipid
  • 60% protein
  • 1-10% Carbohydrate
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2
Q

Describe the structure of a phospholipid molecule

A

Head group - range of polar molecules (aa’s, choline so, amines and sugars)
Fatty acid “tail” - Lots of variety (C16+18 most common), unsaturated, cis double bond creates a kink in chain

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3
Q

What are Glycolipids?

A

Sugar containing lipids

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4
Q

What is Sphingomyelin?

A

Only phospholipid not based on glycerol (when in membrane is very similar to others)

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5
Q

What are Cerebrosides?

A

Glycolipid with sugar monomers as head groups

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6
Q

What are Plasmalogens?

A

Non-classical Phospholipids

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7
Q

What are Gangliosides?

A

Glycolipids with sugar oligosaccharides for head groups

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8
Q

What does the distribution of lipids in the mebrane depend on?

A

Tissue type and function

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9
Q

What two structures do Amphipathic molecules readily form in water?

A

Micelles and Bilayers

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10
Q

What forces and between what regions drive Bilayer formation?

A

Vdws between the hydrophobic fatty acid chains

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11
Q

Name the four ways that lipids can move in a membrane?

A
  • intra-chain motion
  • Axial rotation
  • Lateral diffusion along same plane
  • Flip-Flop
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12
Q

Name the ways membrane proteins can move?

A
  • Lateral movement
  • Rotation
  • Conformational change
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13
Q

What restricts membrane protein movements?

A
  • Cholesterol levels in particular region
  • Associations with other membrane proteins
  • Association with extra-membranous proteins (e.g cytoskeleton)
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14
Q

How do Peripheral proteins bind to the membrane and how can they be removed?

A
  • Electrostatic forces and H-bonds

- pH changes or Ionic strength changes

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15
Q

How are integral membrane proteins bound to the membrane and how can they be removed?

A
  • Interact with hydrophobic region of bilayer

- Agents that compete for hydrophobic interactions (e.g detergents, organic solvents)

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16
Q

How is membrane protein synthesis different to secretory protein synthesis?

A

The protein has to span the membrane not sit solely within it

17
Q

How does a membrane protein achieve its spanning of the membrane in its synthesis?

A

Through the addition of a stop transfer signal which is a highly hydrophobic chain of around 20 aa’s

18
Q

What are Hydropathy plots used for?

A

To see how many transmembrane regions a protein has

19
Q

Why is membrane asymmetry important?

A

Important for biological function

I.e Ensure receptors are situated on the same side of the membrane that their substrate will be

20
Q

Why is the “kink” in the FA chain important?

A

It decreases phospholipid packing and hence increases fluidity of the membrane

21
Q

How does cholesterol increase packing in the membrane?

A

Forms H-bonds with FA chain

22
Q

How does cholesterol decrease membrane fluidity?

A

Decreases the packing by being a physical barrier between chains

23
Q

What is protein lateral diffusion affected by?

A
  • Size
  • Aggregation
  • Association with other proteins (intra or extracellular)
  • Amount of cholesterol in near vicinity
24
Q

What is the erythrocyte cytoskeleton composed of and why is it important?

A

Spectrin and Actin

Maintains shape of RBCs

25
How does the cytoskeleton attach to the membrane?
Ankyrin and Glycophorin Bound to Band 3 and Band 4.1 respectively
26
What are Haemolytic anaemias in general?
RBCs become spherical and are therefore subject to increased lysis due to shearing forces of capillary beds
27
What is Hereditary Spherocytosis?
Spectrin levels depleted, RBCs round up, leads to increased lysis Bone marrow cannot compensate and hence a haemolytic anaemia results
28
What are Amphipathic molecules?
Molecules with both Hydrophobic and Hydrophilic moieties
29
What is Hereditary Elliptocyosis?
Spectrin molecules are unable to form heterotetramers, RBCs form elliploid shape (rugby ball) and a Haemolytic anaemia results