topic 06 biological membranes Flashcards

1
Q

what are a cell’s membrane composed of?

A

lipids, proteins, and carbohydrates

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2
Q

what are the functions of a biological membrane?

A

separates the content of a cell/organelle from its environment

control import and export of molecules using proteins

contains sensors/receptors that allow cells to respond to external stimuli

involved in cell movement

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3
Q

what are lipids insoluble in? soluble in?

A

insoluble in water

soluble in organic solvents

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4
Q

what are the functions of lipids?

A

structural components of biological membranes

energy storage

enzyme cofactors

signaling molecules

pigment

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5
Q

what are the major classes of lipids?

A

fatty acids

triacylglycerol/triglycerides

glycerophospholipids

sphingolipids

steroids

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6
Q

describe the structure of a fatty acid. draw one out with no double bonds!

A

hydrocarbon chain ending in a carboxylic acid group (COOH). usually contains an even number of carbons (4-24)

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7
Q

what are the levels of saturation for hydrocarbon chains?

A

saturated: no double bonds

monosaturated: one double bond

polysaturated: more than one double bond

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8
Q

on a fatty acid, where would the first double bond be? what about additional double bonds? knowing this, are the double bonds cis or trans?

draw a fatty acid with 2 or 3 double bonds

A

the first double bond is USUALLY between carbon 9/10 from the carboxylic acid group

any other double bonds after would usually be added at every 3 carbons. after drawing it out, one can see that the double bonds have a cis conformation and form kinks in the chain

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9
Q

in nutrition literature, how are carbons counted in fatty acid?

A

from the methyl end

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10
Q

describe the structure of a glycerol. draw it.

describe the structure of a triacylglycerol/triglyceride.

A

glycerol is a 3 carbon chain with hydroxyl groups at the end

triacylglycerol has fatty acids attached to the hydroxyl groups through an ester linkage.

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11
Q

what is the function of a triacylglycerol?

A

to store fatty acids as energy reservoirs in adipocytes (fat cells)

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12
Q

describe the structure of glycerophospholipids

A

similar to triacylglycerol but one of the fatty acids replaced with a phosphate group

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13
Q

describe the structure of a sphingolipid

A

based on a sphingosine molecule which contains a large (hydrophobic) hydrocarbon chain. a second chain, a fatty acid chain, is added to its amine group to form a ceramide. this ceramide is modified to make sphingomyelins which form a sphingolipid with monosaccharide groups

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14
Q

describe the structure of a steroid

A

based on a system of 4 fused rings. 3 of these rings have 6 carbons. 1 of these rings has 5 carbons. the ring system is almost planar

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15
Q

describe the structure of a sterol

A

a steroid with a hydroxyl group at C3

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16
Q

why are fatty acids, sphingolipids, and glycerophospholipids ideal for forming biological membranes?

A

they are amphipathic - they have both hydrophobic and hydrophilic parts.

when placed in water they will spontaneously arrange themselves so hydrophilic regions contact water and hydrophobic parts will cluster together in an area protected from water

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17
Q

what happens if the hydrophilic group of the lipid bilayer has a larger diameter than the hydrophobic group?

what if the groups are of equal size?

A

if the hydrophilic portion is larger, the lipid will have be triangular or wedge shaped. these lipids will form a micelle, a circle, so water is excluded from the center

if the portions are of equal size, the lipid bilayer can form in which the hydrophilic heads form two surfaces that contact water and protect the hydrophobic group in the interior

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18
Q

describe the flexibility and fluidity of a lipid bilayer

A

they are flexible bc of the many individual molecules. the flexibility allows them to prevent hydrophobic edges from contacting the water by spontaneously closing to form spherical vesicles or liposomes that enclose the aqueous interior.

the fluidity is caused by the individual lipid molecules that move and diffuse within the plane of the lipid bilayer. the composition of the bilayer is adjusted to maintain optimal fluidity

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19
Q

what are the four factors that determine the fluidity/diffusion rate of the lipid bilayer?

A

temperature: fluidity is high at certain temperatures. below a certain transition temperature, the lipid bilayer will exist in a gel state where its movement is reduced

proportion of unsaturated fatty acyl chains within the phospholipids and glycolipids: CIS double bonds prevent tight packing of the fatty acyl chains, increasing fluidity

length of fatty acyl chains in the phospholipids and glycolipids: shorter chains = more mobility & fluidity

amount of cholesterol in the bilayer: because of the presence of a hydroxyl group, cholesterol is mildly amphipathic. at higher temperatures, increasing the amount of cholesterol in the membrane reduces the fluidity of the bilayer because the cholesterol packs between the other lipid molecules and restricts motion. at lower temperatures approaching phase transition, cholesterol increases fluidity in the bilayer by interfering with the orderly packing of other lipids

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20
Q

describe the composition of the biological lipid bilayer and how this is established

A

it is asymmetrical. the composition of 1/2 of the bilayer’s surface will be different than the other half. however, cholesterol is evenly distributed

the asymmetry is established as lipids are synthesized. the asymmetry is regulated by phospholipid translocases that are either ATP-independent (scramblase) or ATP-dependent (flippases or floppases).

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21
Q

what are the types of diffusion a lipid could undergo within a bilayer?

A

lateral

rotation

flexion

transverse

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22
Q

describe the fluid mosaic model

A

proteins are free to diffuse laterally within the lipid bilayer unless restricted by cellular components

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23
Q

where will one never find carbohydrates on the membrane?

A

on the inside surface

24
Q

why is it easy to maintain the asymmetry of the lipid membrane?

asymmetry for what can lipid not be maintained? why is this so?

A

transverse diffusion is slow

enzymes maintain symmetry but putting lipids back in their place (flippase and floppase) - flippase moves from outer to inner – floppase moves from inner to outer

asymmetry for cholesterol can not be maintained because it has a small polar head that enzymes can’t interact with

25
Q

how much of a typical biological membrane’s mass does proteins make up?

A

40-50%

26
Q

how do proteins associate with the biological membrane?

A

integral

peripheral

lipid linked

27
Q

describe integral membrane proteins

also define transmembrane proteins

A

some portion of a polypeptide chain contacts the hydrophobic interior of the membrane. usually, the peptide chain of the integral membrane protein completely crosses the membrane at least once. a few don’t

integral membrane proteins don’t flip flop

transmembrane proteins: polypeptides having membrane spanning segments. they are exposed to aqueous compartments on both sides (including hydrophobic interior)

28
Q

describe the structure of the transmembrane segment of a protein. why is it like this?

A

they have alpha-helical structures which maximizes the hydrogen bonding between the polar backbone groups while minimizing interactions between the backbone group and hydrophobic interior

29
Q

how many hydrophobic amino acid residues does a single membrane-spanning alpha-helix consist of? why are they hydrophobic?

A

20

the hydrophobic side chains favourably interact with the bilayer’s interior: the alpha-helix doesn’t readily leave bilayer because doing so will expose the hydrophobic side chains to the water

30
Q

describe the beta-barrel structure and its purpose

A

made of beta-strands in transmembrane proteins

the outside of the barrel is covered with hydrophobic side chains while the side chains that project toward the inside are hydrophilic (polar)

31
Q

describe peripheral membrane proteins

A

not embedded into bilayer. they are associated with integral membrane proteins or with the hydrophilic head groups of the membrane lipid. it does not make contact with the hydrophobic interior

32
Q

describe lipid linked proteins

A

one or more lipid molecules covalently attached to the end of the protein or to particular side chains (usually cysteine).

the lipids are embedded into the membrane but the protein itself and the sidechains are not exposed to the interior

33
Q

how can the different types of proteins associated with the membrane be removed? which of these disrupt the bilayer?

A

integral and lipid linked protein removal disrupts the bilayer

integral: detergent, etc

lipid linked: detergent or removing attached lipid, etc

peripheral: can be done under relatively mild conditions that leave the bilayer intact

34
Q

why are integral membrane proteins more difficult to study than water-soluble proteins?

A

their hydrophobic regions must always be covered with lipids or detergents. or else they hydrophobic regions cluster together, causing the protein to aggregate or even precipitate

use of detergent complicates the purification procedure as it may alter secondary, tertiary, and quaternary structure

35
Q

what are glycoproteins? where could they never be found?

A

membrane proteins that are modified by the carbohydrates on asparagine, serine, or threonine side chains - these sugars are never attached to the cytosolic (inside) surface of the proteins

36
Q

what are detergents?

A

amphipathic molecules that disrupt the membrane and coat the hydrophobic parts of the membrane proteins to keep them stable

37
Q

why is the alpha-helix stable in the hydrophobic interior?

A

in the alpha helix, polar backbone molecules bond with each other. since there are no H-bonding groups to bond to, the structure remains stable (transmembrane proteins)

38
Q

describe the cluster of transmembrane alpha-helices

A

hydrophilic interior

hydrophobic exterior

39
Q

what’s needed to satisfy the hydrogen-bonding requirements of a transmembrane protein’s backbone?

A

beta-barrel

side chains of the beta-barrel will be arranged so that the hydrophobic side chains face the lipids while the inside of the beta-barrel may be hydrophilic

40
Q

what are the different functional proteins associated with the biological membrane?

A

channels/transporters

receptors

enzymes

anchors

41
Q

what are the different types of transporter proteins? what do they do?

A

uniporter: transports a single species in one direction

symporter: transports two species in one direction

antiporter: transports two species in opposite directions

42
Q

define facilitated transport

A

in which transport/channel proteins move ions and polar molecules between cell’s compartments or inside/outside a cell.

43
Q

differentiate between transporters and channel proteins

A

transporters: undergo conformational change to move ions/molecules across membrane

channels: when open, they form continuous pores through the bilayer. some channels can open and close through conformational changes

transporters can facilitate active transport; channels perform only passive transport

44
Q

what are porins?

A

beta-barrel proteins that cross the membrane while acting as a pore, allowing molecules to diffuse through.

forms non-specific passageways

45
Q

what can diffuse through a potassium channel? what is it impermeable to?

A

K+ and large monovalent cations such as Rb+

impermeable to small ions: Na+ & Li+

46
Q

describe the electrochemical gradient

A

opposites attract :3

charged species tend to move towards side with opposite charge.

the side with a higher concentration would “leak” to the other side. net movement towards side with a lower concentration.

47
Q

differentiate between passive and active transport

A

passive: if a pathway exists, ions/molecules will move down the electrochemical gradient

active: source of energy used to move ions/molecules. this energy can be from the hydrolysis of ATP (into ADP & phosphate) or other sources

48
Q

describe receptor proteins

A

ions/molecules/ligands bind to the receptor at the binding site

they sense chemical signals on the outside of the cell and carry the message to the inside so the cell can react to the environment - they can recognize specific molecular signals

receptors can also have enzymatic activity. sometimes the receptor itself acts on the signal, or another protein will

49
Q

describe enzyme proteins

A

catalyze chemical reactions

50
Q

describe anchor proteins

A

structural proteins that provide stability to the membrane and helps control the cell’s shape and position relative to other cells

they bind to other macromolecules on one/both sides

51
Q

example given: describe the steps a glucose transporter will take when a glucose binds to it

A
  1. glucose binds to site on the transporter’s exterior
  2. binding of glucose triggers conformational change, exposing the binding site to the interior
  3. glucose dissociates from the transporter
  4. transporter reverts to original conformation
52
Q

why do phospholipids with unsaturated tails make the bilayer more fluid?

A

unsaturated tails are not as straight as saturated tails and thus are less able to pack close together

53
Q

how do glycerophospholipids respond when placed in an aqueous solution?

A

they form spherical liposomes that enclose water

54
Q

what distinguishes transmembrane proteins from lipid-linked integral membrane proteins?

A

all transmembrane proteins have amino acid side chains that are in direct contact with the hydrophobic part of the lipid bilayer; some lipid-linked integral membrane proteins do not.

55
Q

how do membrane proteins move?

A

laterally

rotate across perpendicular axis

CANT tumble (“flip flop”)

56
Q

what type of protein is bacteriorhodopsin (in regards to membrane)?

A

transmembrane

57
Q

why do transmembrane regions of integral membrane proteins stay within the membrane?

A

the transmembrane regions contain hydrophobic side chains that would be exposed to water if they were to leave the membrane