Biomembranes Flashcards

1
Q

What are the basic components of bio membrane

A

Lipids Sterols and protiens

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2
Q

What does amphipathicity do

A

Phospholipis spontaneoutly form lipid bilayers in aqueous solution where the properties of the fatty acids confer properties on bilayers

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3
Q

What does saturated mean

A

No double bonds

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4
Q

What does unsaturated mean

A

One double bond

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5
Q

What does polyunsaturated mean

A

More than one double bond

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6
Q

What changes melting point

A

Increases with chain length decreases with increasing unsaturation

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7
Q

What is a fatty acid

A

Long hydrocarbon chain attached to a polar carboxyl head group

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8
Q

What are properties of biomemembranes

A
  1. Fluid
  2. Closed compartments
    3, Semi permeable
  3. Asymmetric
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9
Q

What makes a membrane more fluid

A

Increase in double bonds
Shorter fatty acids

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10
Q

What effects membrane fludity

A

Steriods
Protiens
Temperature if you are cold blooded
Double bonds
Fatty acid length

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11
Q

How can you measure flourence recovery

A

You bleache a cwertain area the flourcences from outside migrate in and the bleached will start to migrate out indirect measure on fluid things are

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12
Q

What makes fluidit slower

A

Diffusion is 10 x slower in plasma membranes that contain protiens than pure bilayers

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13
Q

What does cytosolic face mean for plasma membrane

A

Internal face

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14
Q

What does cytosolic face mean for vesicle membrane

A

External face

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15
Q

Where is the exoplasmic face

A

always facing the inside

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16
Q

What can pass through

A

Small uncharged or hydrophobic molecules pass freely

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17
Q

What cant pass through

A

Large hydrophillic or charged molecules

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18
Q

Where are carbohydrates found

A

Exclusively on the exoplasmic face

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19
Q

Where are protiens

A

Either embedded in the bilayer in a fixed orientation or are associated with only one side

20
Q

What are the three types of membrane protiens

A

Intergral
Lipid linked
Peripheral

21
Q

What are the three domains of integral membrane protiens

A

Cytoplasmic (hydrophilic)
(often amion acids such as Argo or lys)
transmembrane a or helix or b bareel
Exoplasmic domains are glycosylated

22
Q

How many amino acids are alpha helix

23
Q

What are lipid linked protiens

A

They have a GPI anchor
the exoplasmic requires sugar residues

24
Q

What is acylation

A

Aclyation attaches through N-termial of GLy

25
What is prenylation
Attaches cys residuce at c terminus
26
What are some characterstics of lipid-linked protiens
Protien does not eneter bilayer Has lateral mobility in membrane
27
What are peripheral protiens attached by
Attached through non-covalent interactions Ionic interactions hydrogen bonds Protien-protien interacations Van der wall forces
28
How can intergral protiens link to cytoskelton
Usin peripheral membrane protiens
29
Where does translation occur
In the cytoplasma Ribsomes will translate and continue to translate in the cytoplasam unless it has a reason not ot
30
What does translation start with
N terminal domain N terminal single is cleaved and that is what tells the protien to go to the ER
31
What is STA
Stop transfer/membrane anchor sequence only be used to change protien from ER lumen to cytosol
32
What is SA
Single anchor internal uncleaved sequecence
33
What does a topogenic sequence do
Tell the ribsome what to do
34
What are tail anchored protiens require
Get3 recognition of hydrophobic C-terminal tail, membrane embedded Get 1 adn 2 and Atp hydrolosys
35
What are the steps of Tail anchored protiens
Hydrophobic c-terminal tail Gets recgonized by Get3 and take it to the Er Ger1 and Get 2 are also there Using atp hydrolis it shoves the hydrophobic part into the membrane no extracellular domain Inserts hydrophobic tail and becomes an integral protien
36
What are the steps of the type 1 protiens
1. Translate N terminal sequence into the Er recognize the topogenic sequence then it is recognized to take to ER lumen 2. Protien peptidase puts into a translocon 3. Sequence gets cleavedoff 4. N terminal domain if not other sequence would just be a lumen 5. Get to the STA this a TM domain gets transfered 6. Rest of the peptide is translated in the cytosol
37
Steps of GPI- anchored protien
Starts like Type 1 portiens with N terminal in lumen and C terminal STA Sequence near membrane is recognized by GP1 trasamidase which cleaves and transfers the luminal portion to the adjacent GPI Later mobility Since the STA is very close to the carboxyicl end it had no protien in the cytsol
38
Synthesis of type 2 and type 3 protiens
have a SA Orientation is determined by the positvely charged amion acids
39
What end is in the cytsol in type 2
NH3
40
What end is in the cytsol for type 3
COO
41
How do you know which part will be in the cytsol
Have the charged particle right next to the NH3 that side will be in the cytsol mean it is in the type 2 If the charge comes after the SA then the NH3 will be in the lumen and the COO in the cytsol
42
Syntheis of Type 4 protiens
Orientation of initial helix is determined by positively charged amino acids next to signle anchor sequence Have alternating SA and STA Even or odd transmembrane domains
43
What is type one
STA signal sequence gets cleaved and the NH3 ends up in the lumen
44
What is type 2
Has an SA which an internal single that tells you where to go this is where the chared is on the NH3 side and it ends up in the cytsolol
45
What is type 3
The charge is on the side of after the SA and the COO is ending up in the cytsol
46
What is type 4 A
The positve charge is before the SA which makes the amino side in the cytsol and the COO is in the lumen and then it switches at the next STA
47
What is type 4 B
You have 2 SA in a row The spaces are the same You have more Sa in the row Start in the lumen