2 - Lipids and Proteins in Membranes Flashcards

1
Q

What is the function of a membrane?

A
  • Selectively permeable barrier
  • Communication
  • Control of enclosed environment
  • Recognition (signalling molecules)
  • Signal generation, e.g electrical
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2
Q

Are all membranes the same?

A

No, specialised for function, e.g mitochondria different to cell membrane. Different parts of same membrane can be different too

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3
Q

What is the membrane composition (dry)?

A
  • 60% protein
  • 40% lipid
  • 1-10% carbohydrate

Water makes up 20% wet weight

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4
Q

What is the main property of membrane lipids that makes them suitable for their function?

A

Amphipathic

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5
Q

What is the structure of a phospholipid?

A

Head: Small and polar. Can have small attachements, e.g choline

Tail: C14-C24, C16/18 most popular so uniform thickness. Unsaturated bonds, cis, cause kink to increase fluidity

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6
Q

What is the exception to the phospholipid structure?

A

Sphingomyelin. Not based on glycerol.

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7
Q

How do you make a glycolipid?

A

Take of phosphocholine head and replace with sugar.

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8
Q

How do lipids arrange themselves in water?

A
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9
Q

How do phospholipids move in the membrane?

A
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10
Q

How are membranes kept dynamic?

A

Cholesterol and cis bonds.

Reduce phospholipid packing

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11
Q

What is the structure of cholesterol and what is it’s function?

A

Regulate fluidity. Need in diet for membrane integrity.

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12
Q

How do proteins move and how can they be restricted?

A
  • Everything but flip-flop (too large, need lots of KE and wouldnt do function, e.g LGIC wrong way)
  • Aggregates
  • Bound to cytoskeleton
  • Cell adhesion
  • High cholesterol areas
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13
Q

What is the evidence for membrane proteins?

A
  • Facilitated diffusion
  • Ion gradients
  • Specificity of cell responses
  • Freeze fracture (heavy metal, snow drift EM, E AND P FACE)
  • Fractionation and Gel electrophoresis
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14
Q

What types of proteins are in the membrane and how are they removed?

A

Peripheral: Associated by H-bonds and electrostatic attractions. Removed by pH or ionic change, e.g salt wash

Integral: Associated with hydrophobic area. Removed by agents that compete for non-polar interactions and destroy membrane, e.g solvent/detergent

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15
Q

What is hydropathy?

A

Can tell shape of membrane protein, hydrophobic parts in membrane and hydrophilic out

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16
Q

What is toplogy of membrane proteins?

A

Membrane proteins always orientated one way for efficiency

17
Q

What does the erythrocyte skeleton consist of?

A

A rigid lattice of long spectrin molecules adhered to transmembrane proteins by peripheral attachment proteins, preventing lysis

18
Q

How can you tell what membrane proteins are in the erythrocyte membrane?

A

Ghost membranes. Only transmembrane are Glycophorin A and Band 3

19
Q

What is spectrin?

A

Tetramer protein of 2 A and 2 B. Tethered to cell membrane to maintain integrity

20
Q

What are two types of haemolytic anaemias due to poor functioning of the cytoskeleton?

A
  • Hereditary Spherocytosis - Lack of spectrin so cells appear spherical. More prone to lysis, cleared by spleen
  • Heriditary Elliptocytosis - Defective spectin, heterotetramers cannot form so cells are fragile and rugby ball shaped, lysis

Treatment: Blood transfusion

21
Q

Why is the membrane asymmetrical?

A

Different compositions and functions

22
Q

How are secretory proteins synthesised?

23
Q

How are proteins for the inside of the cell made?

A

In the ribosome in the cytoplasm, there is no signal sequence

24
Q

How are membrane proteins produced?

A
  • Same as secretory proteins
  • Hydrophobic stop transfer signal reached
  • Ribosome detaches and completes synthesis in cytoplasm
  • ER –> Cis Golgi –> Trans Golgi –> Vesicle –> Fuse with membrane, same as before
25
What determines where N and C terminal are?
Signal Peptidase: N in, C out No cleavage: C in, N out
26
What is the role of band 3 and glycophorin A?
Integral proteins that prevent flip flop rotation
27
What property does spectrin give erythrocytes?
Allows them to be rigid but flexible, holding their shape
28
What do ankyrin and band 4.1 do?
Attach spectrin to integral proteins, restricting lateral mobility
29
How do membrane bilayers form in water?
- Liposomes - Form spontaneously - Non covalent vdw forces between hydrophobic tails - Hydrogen bonds between hydrophilic heads