Chapter 4: 4.6 Membrane Protein Function - Specifics Flashcards

1
Q

Define:

Bacteriorhodopsin (bR)

A

A light fueled proton pump found in halobacterial membranes (consist of ~75% of membrane)

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

What type of membrane protein is bacteriorhodopsin?

A

A multi-spanning membrane protein

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

Membrane proteins are hard to…

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

Can membrane proteins be studied with NMR?

A

No, membrane proteins need to be removed from the membrane with detergents making them too large for NMR

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

The purity and abundance of bR in the membrane provide an opportunity to study…

A

The crystal structure of a membrane protein

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

How many transmembrane alpha-helices surround a chromophore?

A

7

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

What surrounds a chromophore?

A

7 transmembrane alpha-helices

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

In non-activated bR:

Describe the structure of bR

A

A retinal molecule is bound to a key Lys residue

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

True or False:

The retinal in non-activated state is in cis conformation

A

False, everything is in trans conformation

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

What is the key Lys residue in bR known as?

A

Schiff base

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

List:

The steps of light activation of bR (5)

A
  1. Light causes the C-13 to take on a cis conformation
  2. The conformational change results in proton transfer to a nearby Asp )Asp85) and proton release from Glu194/Glu204 pair
  3. The Schiff base acquires a proton form Asp96
  4. Asp96 takes up a proton from the cytosol
  5. Asp85 re-protonates the Glu194/Glu204 pair resetting the system
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What is the light activation process of bR known as?

A

“Proton hopping”

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

Is “proton hopping” faster or slower than diffusing?

A

Faster

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

State:

Structure of porins

A

Consist of beta-barrels

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

Where are porins located?

A

Located in outer-membranes of cells and organelles

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

What can pass through porins?

A

Small hydrophilic molecules pass through

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

Describe:

The amino acids in strands in the porins

A

Alternate between polar and non-polar
* Polar amino acids face inwards
* Non-polar amino acids face outwards

18
Q

What can some bacteria use porins for?

A

Can use porins to lyse host cells

19
Q

Describe:

The process of bacteria lysing cells using porins

A
  1. 7 identical beta sheet pairs (beta-turn-beta) are added into a host membrane creating a pore
  2. Cell contents spill out
20
Q

List:

The two types of diffusion

A
  1. Passive Diffusion
  2. Facilitated Diffusion
21
Q

Define:

Passive Diffusion

A

Not facilitated by transporter proteins

22
Q

What can move through in passive diffusion?

A

Small, uncharged molecules
* Move WITH their concentration gradient (from high to low concentration)

23
Q

Define:

Facilitated Diffusion

A

Integral proteins transport molecules in a thermodynamically favourable direction

24
Q

What special behaviour does facilitated diffusion exhibit?

A
  • Can be very specific in their cargo
  • Exhibit saturation behavior
25
Q

Define:

Ion Channels

A

Very selective for their respective ions

26
Q

True or False:

Ions move at a slow rate through ion channels

A

False, ion channels move ions at very high rates (10^8 per second)

27
Q

Describe:

Ion Channels

A

They are gated, meaning they have an open and closed state

28
Q

Define:

Potassium Ion Channels

A

Play a key role in electrical impulse formation in neurons
* Has additional roles

29
Q

Describe:

Structure of Potassium Ion Channels

A

Made up of 4 identical subunits (predominantly alpha-helices)

30
Q

Describe:

Structure of each subunit of a Potassium Ion Channels

A

Has 5 key amino acids lining the active site (TVGYG)

31
Q

Describe:

Structure and Purpose of the opening for Potassium Ion Channels

A

Opening of the small size
* Forces these resides to replace the water that surrounds the ion extracellularly
* Size specific for K+

32
Q

How is a Potassium Ion Channel opened/closed?

A

Can be opened/closed via a conformational change in a conserved glycine residue

33
Q

State:

The steps that Receptors undergo when they act

A
  1. Bind or “sense” an extracellular stimuli
  2. Transmit to secondary messengers
  3. Cell responds
34
Q

Define:

GPCR

A

G-Protein-Coupled Receptors

35
Q

What can GPCR bind to?

A

Both natural and synthetic stimuli (ligands)

36
Q

In GPCR, what are signals transduced by?

A

GTP binding proteins

37
Q

Describe:

G-proteins in GPCR

A

Hertero-trimers consisting of α, β, and γ subunits

38
Q

In a GPCR:

Describe what happens once a ligand binds to the receptor

A

The α subunit binds GTP and dissociates from the βγ subunits

39
Q

In GPCR:

The dissociation of α subunit leads to what?

A
  • Activates an effector enzyme
  • Causes a series of enzymatic events in the cell
  • Ultimately leads to cell response
40
Q

True or False:

Signals by GPCRs can be amplified

A

True

41
Q

How can signals by GPCRs be amplified?

A

One hormone-receptor complex can activate more than one G-protein

42
Q

In GPCRs:

How are GPCRs turned off?

A
  1. GTP converted to GDP during activation of the effector enzyme
  2. Brings the α subunit back into complex with the βγ subunits