S1 Flashcards

1
Q

What are the functions of biological membranes?

A
  • highly selective permeabilty barrier
  • Control of the enclosed chemical environment
  • communication
  • recognition-signalling molecules
    i. Adhesion proteins
    ii. Immune surveillance
  • signal generation in response to stimuli (electrical, chemical)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

Dry weight general membrane composition

A

40% lipid
60% protein
1-10% carbohydrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Membranes are hydrated structures. What is the total weight of water in membranes?

A

20%

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What are the four different types of phospholipid head groups?

A

Choline, Serine, Ethanolamine and Inositol

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Name a phospholid with a special head group

A

Sphingomyelin

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Name two types of glycolipids

A

Cerebroside

Ganglioside

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

What is the difference between cerebrosides and ganglioside?

A

C: Lipids with head group sugar monomer whereas G: Lipids with head group oligosaccharide (sugar multimers).

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Draw a lipid micelle

A

Image

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Image

A

Lipid micelle

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What is liposome?

A

Lipid bilayer around a cell

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Draw a lipid bilayer

A

Image

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What motions are possible with phospholipids?

A

Flexion, rotation, flip flop (rare) and lateral diffusion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What influence does a cis double bond have in bilayer structure?

A

Reduces phospholipid packing so increases fluidity.

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Describe the structure of cholesterol

A

Polar head group on top of a rigid planar steriod structure with a non-polar hydrocarbon tail.

Image

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What’s the effect of cholesterol concentration on the endothermic phase transition of phospholipid bilayers?

A

As cholesterol concentration increases endothermic phase transition decreases.

Image

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Where does cholesterol insert and bind in the phospholipid bilayer?

A

Cholesterol inserts between the hydrophobic tails of phospholipids and the polar OH group of the cholesterol binds to the double bonded O of the ester group in the phospholipid.

17
Q

How does cholesterol restrict motion of phospholipid tails?

A

The upper region of the phospholid tail is aligned with the rigid steriod structure of cholesterol so it’s motion is restricted. However, the lower region of the phospholid tail is aligned with the non polar hydrocarbon tail of the cholesterol so its motion is unaffected.

18
Q

Explain the paradoxical effects of cholesterol in phospholipid bilayers

A

Cholestrol descrease fluidity of the bilayer by reducing phospholid chain motion but also increases fluidity of the bilayer by reducing phospholid packing.

19
Q

What is the functional evidence for proteins in membranes?

A
  • Facilitated diffusion
  • Ion gradients
  • specificity of cell responses
20
Q

What are the biochemical evidence for protein s in membranes?

A
  • Membrane fractionation + gel electrophoresis

- Freeze Fracture

21
Q

What can be used to make the membrane fractionation+ gel electrophoresis?

A

SDS-Polyacrylamide gel electrophoresis (SDS-PAGE)

22
Q

Describe how freeze fracture works

A

Cell is frozen in water and then fractured with a knife to produce an E fracture face and a P fracture face.

23
Q

What are the three modes of motion permitted for proteins?

A

Conformational change
Rotational
Lateral

24
Q

What mode of action is not permitted for proteins? And why?

A

Flip-flop because it is not thermodynamically favourable.

25
Q

What are the three ways in which membrane proteins’ mobility can be restricted?

A

Aggregates
Tethering
Interaction with other cells

26
Q

How does lipid mediated effects restrain mobility?

A

Proteins tend to separate out into the fluid phase or cholesterol poor regions.

27
Q

What are the two types of membrane proteins?

A

Peripheral and integral

28
Q

What are the differences between peripheral and integral membranes proteins?

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 or ionic strength
  • Are removed by agents which compete for non-polar interactions
29
Q

What agents will compete with integrals for non-polar interactions?

A

Detergents and organic solvents

30
Q

The lipid mosaic model of membrane structure is also known as what?

A

Singer-Nicholson model

Image

31
Q

What are two key features about the structure of transmembrane polypeptide?

A
  • R groups of amino acid residues in transmembrane domains are largely hydrophobic
  • transmembrane domains are often alpha helical.
32
Q

How is the erythrocyte’s shape maintained?

A

The erythrocyte’s shape is held together by the cytoskeleton.

33
Q

How is spectrin lattice anchored? (detailed)

A

Band 3 and Glycophorin A (transmembrane proteins) anchor spectrin lattice adhered through ankyrin and Band 4.1 which are attachment proteins.

Image

34
Q

How is the spectrin lattice anchored?(general)

A

transmembrane proteins anchor spectrin lattice adhered through attachment proteins.

Image

35
Q

Examples of haemolytic anaemias

A

Hereditary Spherocytosis

Hereditary Elliptocytosis

36
Q

What is hereditary spherocytosis?

A

Spectrin is depleted by 40-50% causing erythrocytes to round up. This means less resistance to lysis and clearance by spleen.

37
Q

What is hereditary Elliptocytosis?

A

Defect in spectrin molecule where there is no hereterotetramer formation so fragile elliptoid cells (look like rugby balls)