Membranes and Receptors Flashcards

0
Q

Define amphipathic

A

Contains both hydrophobic and hydrophilic moieties

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1
Q

What are the main kinds of lipids in plasma membranes?

A

Phospholipids
Glycolipids
Cholesterol

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2
Q

Describe a phospholipid

And the range of head groups it may have

A

Glycerol backbone
Two fatty acid tails
Phosphate
Polar head groups could be choline, amines, amino acids and sugars

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3
Q

What to cis double bonds do in phospholipids?

A

They reduce the packing between adjacent phospholipids

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4
Q

Describe plasmalogens and give an example

LOOK OVER AGAIN AND EDIT

A

Non classical phospholipids such as sphingomyelin

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5
Q

What is the difference between cerebrosides and gangliosides?

A

Both are glycolipids
Cerebrosides: head group is a sugar monomer
Gangliosides: head group is an oligosaccharide

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6
Q

What are some general functions of membranes?

A
Barrier: continuous and highly selective
Control of enclosed chemical environment
Communication: ECF/ICF
Recognition: signalling molecules, adhesion, immune surveillance
Signal generation in response to stimuli
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7
Q

What is the composition of a membrane?

Percentages dry weight

A

40% lipid
60% protein
1-10% carbohydrate
Water when hydrated 20% total weight

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8
Q

What sort of movement can lipids do in bilayers?

A

Intrachain motion: cis formation increases fluidity
Fast axial rotation
Fast lateral diffusion
Flip flop - rare

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9
Q

What are some functions of membrane proteins?

A
Enzymes
Transporters
Pumps
Ion channels
Receptors
Energy transducers
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10
Q

Give evidence for proteins in membranes

Functional and biochemical

A

Functional: facilitated diffusion, ion gradients, specificity of cell responses
Biochemical: membrane fractionation, freeze fracture

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11
Q

What sorts of protein mobility exist in bilayers?

A

Conformational change
Rotational
Lateral
NO FLIP FLOP: hydrophilic through hydrophobic region not energetically favourable

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12
Q

What restrains protein mobility in a bilayer?

A

Membrane protein associations make movement sluggish
Proteins prefer cholesterol poor regions, fluid phase
Tethering to the cytoskeleton, other cells, basement membrane, peripheral proteins

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13
Q

What is a peripheral protein?

A

Associated with the surface
Bound by electrostatic/H bond interactions
Remove with changes in pH or ionic strength

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14
Q

What is an integral protein?

A

Interacts extensively with hydrophobic regions of the lipid bilayer
Can not remove by changing pH or ionic strength
Can remove with detergents or organic solvents which compete for non polar interactions
Hydrophobic R group residues mainly, alpha helical
1 or many hydrophobic domains

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15
Q

Why is membrane asymmetry important?

A

Important for function
Receptors for hydrophobic extracellular messenger molecules
Needs to face ECF

16
Q

Describe how secreted proteins are synthesised

ESA1

A

Free ribosome
Hydrophobic N terminal sequence
Binds SRP, stops protein synthesis
GTP SRP binds to SRP receptors on the ER
SRP dissociates, protein synthesis continues
Protein into ER pore via PTC
Signal cleaved and the ribosome is recycled

17
Q

Describe membrane protein biosynthesis

A

Ribosomes start synthesising, hydrophobic N terminal sequence first
Binds SRP, stops synthesis and binds the SRP receptor, releases SRP
Continues protein synthesis, PTC interacts with signal, further synthesis through the ER
Ribosome is anchored to the pore, hydrophobic a helical area translated
Release of protein and ribosome from PTC, biosynthesis continues in the cytoplasm

18
Q

What does a hydropathy plot show?

A

The number of transmembrane domains in an integral membrane protein

19
Q

How is a membrane protein orientated?

GO OVER WITH MMF NOTES

A

Positive residues at the C end, N into the lumen
Positive residues at the N end, C into the lumen
Delivered to the membrane by the fusing of vesicles, same orientation as in ER

20
Q

Shat is the effect of unsaturated fatty acids in a membrane?

A

Cis double bond
Kink in the chain
Can not pack as tightly
More fluid

21
Q

Describe the structure of cholesterol

A

Polar OH head
Rigid steroid ring structure
Non polar hydrocarbon tail

22
Q

How does cholesterol increase fluidity?

A

Reduces the packing of phospholipids

Stops crystalline structure at low temperatures

23
Q

How does cholesterol reduce membrane fluidity?

A

Reduces chain motion on phospholipids
Rigid sterol structure
Reduces motion at high temps

24
Q

Describe erythrocyte membranes and how they are broken down

A

Over 10 major proteins, most released by changing pH or ionic strength, peripheral, cytosolic
Band 3 and 7 only removed by detergents, so are integral

25
Q

What is the importance of the cytoskeleton in RBCs?

A

Without it the RBCs round up
Lysed by shearing forces in the capillary bed
Cleared by the spleen, haemolytic anaemias

26
Q

What is hereditary spherocytosis?

A

Mutation in the spectrin allele, depletes it by 40-50%
Also can be mutated cytoskeletal elements, dysfunctional binding sites
RBCs round up, increased cell lysis
Bone marrow can not compensate
Haemolytic anaemia

27
Q

What is hereditary elliptocytosis?

A

Common defect in spectrin molecule
Can not form stable heterotetramers
Fragile elliptoid cells
Haemolytic anaemia

28
Q

What is the function of the RBC cytoskeleton?

A

Restricts laral mobility of integral membrane proteins

Also gives the cell flexibility, important to get through capillaries

29
Q

What is the main make up of the RBC cytoskeleton?

FINISH WITH LAST SESSION 1 page

A

Network of spectrin and actin

Adducin cross links spectrin