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CHAPTER 11

MEMBRANE STRUCTURE
2004 Garland Science Publishing
The i!id Bila"er
11-1 For each of the following sentences, fill in the blanks with the best word or phrase
selected from the list below. Not all words or phrases will be used; each word or phrase
should be used only once.
The specialized functions of different membranes are largely determined
by the __________________ they contain. Membrane lipids are
__________________ molecules, composed of a hydrophilic portion and
a hydrophobic portion. ll cell membranes ha!e the same
__________________ structure, with the __________________ of the
phospholipids facing into the interior of the membrane and the
__________________ on the outside. The most common lipids in most
cell membranes are the __________________. The head group of a
glycolipid is composed of __________________.
amphipathic hydrophobic phosphatidylserine
cholesterol lipid bilayer phospholipids
fatty acid tails lipid monolayer proteins
glycolipids lipids sterols
hydrophilic head groups phosphatidylcholine sugars
11-2 "hich of the following membrane lipids does not contain a fatty acid tail#
$a% &hosphatidylcholine
$b% glycolipid
$c% &hosphatidylserine
$d% 'phingomyelin
$e% (holesterol
11-3 "hich of the following statements regarding lipid membranes is T)*+#
$a% &hospholipids will spontaneously form liposomes in nonpolar sol!ents.
$b% ,n eucaryotes, all membrane-enclosed organelles are surrounded by one lipid
bilayer.
$c% Membrane lipids diffuse within the plane of the membrane.
$d% Membrane lipids fre.uently flip-flop between one monolayer and the other.
$e% The preferred form of a lipid bilayer in water is a flat sheet with e/posed edges.
1#$
11-4 bacterium is suddenly e/pelled from a warm human intestine into the cold world
outside. "hich of the following ad0ustments might the bacterium make to maintain the
same le!el of membrane fluidity#
$a% ,ncrease the length of the hydrocarbon tails in its membrane phospholipids.
$b% ,ncrease the proportion of unsaturated hydrocarbon tails in its membrane
phospholipids.
$c% ,ncrease the proportion of hydrocarbon tails with no double bonds in its
membrane phospholipids.
$d% 1ecrease the amount of cholesterol in the membrane.
$e% 1ecrease the amount of glycolipids in the membrane.
11-5 "hich of the following statements regarding the fatty acid tails of phospholipids is
F2'+#
$a% &hospholipids with unsaturated tails make the bilayer more fluid because the tails
contain fewer hydrogen atoms and thus form fewer hydrogen bonds with each
other.
$b% 'aturated phospholipid tails pack more tightly against each other than do
unsaturated tails.
$c% Most membrane phospholipids ha!e one fully saturated tail.
$d% &hospholipid tails in a membrane can interact with each other !ia !an der "aals
interactions.
$e% Fatty acid tails !ary in length.
11-6 New membrane synthesis occurs by
$a% the spontaneous aggregation of free phospholipids into a new bilayer in the
a.ueous en!ironment of the cell.
$b% incorporation of phospholipids into both faces of a pree/isting membrane by
enzymes attached to each face.
$c% incorporation of phospholipids into one face of a pree/isting membrane and their
random redistribution to both faces by flippases.
$d% incorporation of phospholipids into one face of a pree/isting membrane and their
specific redistribution by flippases.
1#%
11-7 Three phospholipids 3, 4, and 5 are distributed in the plasma membrane as indicated in
Figure 677-8. For which of these phospholipids does a flippase probably e/ist#
Figure 677-8
$a% 3 only
$b% 5 only
$c% 3 and 4
$d% 4 and 5
$e% 3 and 5

11-8 "here does most new membrane synthesis take place in a eucaryotic cell#
$a% ,n the 9olgi apparatus
$b% ,n the endoplasmic reticulum
$c% ,n the plasma membrane
$d% ,n the mitochondria
$e% :n ribosomes
11-9 small membrane !esicle containing a transmembrane protein is shown below. ssume
this membrane !esicle is in the cytoplasm of a cell.
Figure 677-;
. 2abel the cytosolic and non-cytosolic faces of the membrane !esicle. This
membrane !esicle will undergo fusion with the plasma membrane.
<. 'ketch the plasma membrane after !esicle fusion, indicating the new location of
the !esicle membrane and the transmembrane protein carried by the membrane
!esicle.
(. :n your drawing for <, label the original cytosolic and noncytosolic faces of the
!esicle membranes as it resides in the plasma membrane. lso label the
e/tracellular space and the cytosol. ,ndicate the amino and carbo/yl terminus of
the inserted transmembrane protein.
1##
11-10 "hy are glycolipids found on the e/tracellular, but not the cytoplasmic, surface of the
plasma membrane#
$a% Flippases transport them from the cytosolic face.
$b% The enzymes that produce them are present only on the e/tracellular surface of
the plasma membrane.
$c% The enzymes that add the sugar groups are confined to the inside of the
endoplasmic reticulum and the 9olgi apparatus.
$d% The oligosaccharides on glycolipids are clea!ed off by enzymes found only in the
cytosol.
$e% They flip spontaneously, after incorporation, due to the hydrophilic sugar head
groups.
Me&brane Pr'(eins
11-11 group of membrane proteins, which can be e/tracted only from membranes using
detergents, are all found to ha!e a similar amino acid se.uence at their carbo/yl terminus=
->>>>>33( $where > stands for lysine, 3 stands for any amino acid, and ( stands for
cysteine%. This se.uence is essential for their attachment to the membrane. "hat is the
most likely way in which the carbo/yl-terminal se.uence attaches these proteins to the
membrane#
$a% The cysteine residue is co!alently attached to a membrane lipid.
$b% The peptide spans the membrane as an heli/.
$c% The peptide spans the membrane as part of a sheet.
$d% The positi!ely charged lysine residues interact with an acidic integral membrane
protein.
11-12 strain of bacteria secretes a to/in that can lyse human red blood cells. 4ou are able to
partially purify the to/in and find that it is a small protein. Furthermore, the to/in is
capable of rendering liposomes made of pure phospholipids permeable to many different
ions. "hat type of protein is the bacterial to/in likely to be#
$a% flippase
$b% -barrel protein
$c% protease
$d% protein containing a single hydrophobic heli/.
$e% n enzyme that adds carbohydrate groups to lipids.
1#)
11-13 For each of the following sentences, fill in the blanks with the best word or phrase
selected from the list below. Not all words or phrases will be used; each word or phrase
should be used only once.
There are se!eral ways that membrane proteins can associate with the cell
membrane. Membrane proteins that e/tend through the lipid bilayer are
called __________________ proteins and ha!e __________________
regions that are e/posed to the interior of the bilayer. :n the other hand,
membrane-associated proteins do not span the bilayer and instead
associate with the membrane through an -heli/ that is
__________________. :ther proteins are __________________ attached
to lipid molecules that are inserted in the membrane.
__________________ membrane proteins are linked to the membrane
through nonco!alent interactions with other membrane-bound proteins.
amphipathic hydrophilic nonco!alently
cortical hydrophobic peripheral
co!alently integral transmembrane
detergent micelle unfolded
11-14 "hich of the following statements regarding membrane proteins is F2'+#
$a% ,ntegral membrane proteins often precipitate $form insoluble aggregates% in
a.ueous solutions lacking detergents.
$b% 'ome hydrophobic amino acids in membrane proteins are not in contact with the
lipid bilayer.
$c% &eripheral membrane proteins can be dissociated from membranes using a gentle
detergent.
$d% 'trong detergents can completely unfold both membrane and nonmembrane
proteins.
$e% ,n transmembrane proteins that form an a.ueous pore through the membrane, the
pore is lined with hydrophobic amino acid side chains.
11-15 &roteins often span the plasma membrane as an - heli/. ,f it takes ?@ amino acids to
span a lipid bilayer, which of the three ?@-amino acid se.uences listed below is the most
likely candidate for such a transmembrane segment# +/plain your choice.
$a% , 2 , A F 9 A F 9 A , 9 9 , 2 2 , '
$b% > , T & A A > B > B 1 > , 1 T & 2 2 , )
$c% 1 T 4 4 4 ) ) ) + 1 1 1 1 1 2 2 , ' 1
1#*
11-16 &roteins that form a C-barrel pore in the membrane ha!e se!eral C-strands that span the
membrane. The amino acid side chains facing the inside of the pore would be
hydrophilic whereas the amino acid side chains facing the lipid bilayer would be
hydrophobic. "hich of the three 7@-amino acid se.uences listed below is the most likely
candidate for a transmembrane C-strand in a C-barrel protein# +/plain your choice.
$a% 1 F > 2 ' A + 2 T
$b% F 2 A 2 1 > ' + T
$c% F 1 > 2 A ' + 2 T
11-17 "hich of the following functions does the cell corte/ perform#
$a% ,t influences the passage of small molecules into and out of the cell.
$b% ,t allows cells to change shape and to mo!e.
$c% ,t lubricates the cell.
$d% ,t restricts the mo!ement of certain proteins in the lipid bilayer.
$e% ,t supports and strengthens the membrane.
11-18 4ou ha!e isolated two mutants of a normally pear-shaped microorganism that ha!e lost
their distincti!e shape and are now round. :ne of the mutants has a defect in a protein
you call and the other has a defect in a protein you call <. 4ou grind up each type of
mutant cell and normal cells separately and separate the plasma membranes from the
cytoplasm. 4ou then wash the membrane fraction with a low concentration of urea
$which will unfold proteins and disrupt their ability to interact with other proteins% and
centrifuge the mi/ture. The membranes and their constituent proteins form a pellet while
the proteins liberated from the membranes by the urea wash remain in the supernatant.
"hen you check each of the factions for the presence of or <, you obtain the results
gi!en below.
First cell e/tract fter urea wash and centrifugation
Membrane (ytosol Membrane 'upernatant
Normal cells and < no or < <
Mutant < no or <
Mutant < < no or <
"hich of the following statements are consistent with your results#
$a% &rotein is an integral membrane protein that interacts with <, a peripheral
membrane protein that is part of the cell corte/.
$b% &rotein < is an integral membrane protein that interacts with , a peripheral
membrane protein that is part of the cell corte/.
$c% &roteins and < are both integral membrane proteins.
$d% The mutation in affects its ability to interact with <.
$e% The mutation in affects its ability to interact with the membrane.
1)0
11-19 1etergents and phospholipids are both amphipathic molecules. Bowe!er, when e/posed
to water, detergents aggregate into small clusters called micelles while phospholipids
form closed spherical liposomes. +/plain what the difference is between the structure of
a detergent compared to the structure of a phospholipid that causes detergents to form
micelles instead of liposomes.
11-20 1i!ersity among the oligosaccharide chains found in the carbohydrate coating of the cell
surface can be achie!ed in which of the following ways#
$a% Aarying the types of sugar monomers used
$b% Aarying the types of linkages between sugars
$c% Aarying the number of monomers in the chain
$d% Aarying the number of branches in the chain
$e% ll of the abo!e
11-21 "hich of the following statements about the carbohydrate coating of the cell surface is
F2'+#
$a% ,t is not usually found on the cytosolic side of the membrane.
$b% ,t can play a role in cell-cell adhesion.
$c% The arrangement of the oligosaccharide side chains are highly ordered, much like
the peptide bonds of a polypeptide chain.
$d% 'pecific oligosaccharides can be in!ol!ed in cell-cell recognition.
$e% ,t can protect the cell surface from mechanical and chemical damage.
11-22 (ell membranes are fluid and thus proteins can diffuse laterally within the lipid bilayer.
Bowe!er, sometimes the cell needs to localize proteins to a particular membrane domain.
Name three mechanisms a cell can use to restrict a protein to a particular place in the cell
membrane.
1)1
H'+ ,e -n'+. Measuring Me&brane /l'+
11-23 Fluorescence reco!ery after photobleaching $F)&% is a techni.ue that allows
!isualization of diffusion within the membrane. 4ou set out to perform F)& using four
different samples of cells. ,n sample 7, you ha!e fluorescently labeled a phospholipid. ,n
samples ?, D, and E you ha!e fluorescently labeled membrane proteins 3, 4, and 5,
respecti!ely. 4ou photobleach an area of the membrane in each sample and record the
rate of reco!ery of fluorescence. The data you obtain are shown in the graphs below=
Figure 677-?D
. *sing the data from these graphs, list the proteins in order of their ability to
diffuse in the membrane, from fastest to slowest.
<. 9i!en the data on the graphs abo!e, is the following statement a good hypothesis=
protein 3 and protein 5 are always present in the cell as part of the same protein
comple/# +/plain your answer.
1)2
11-24 4ou perform single-particle tracking $'&T% e/periments on three proteins, , <, and (,
and obtain the following pathways=
Figure 677-?E
. "hich protein displays a pattern of motion similar to a protein that is anchored to
the cytoskeleton#
<. ,f you were to find a cell containing a membrane where 7@F of its membrane
proteins were anchored to the cytoskeleton, how do you think this would affect
the fluidity of the lipids in the membrane#
1)0
Ans+ers
11-1 The specialized functions of different membranes are largely determined by the proteins
they contain. Membrane lipids are amphipathic molecules, composed of a hydrophilic
portion and a hydrophobic portion. ll cell membranes ha!e the same lipid bilayer
structure, with the fatty acid tails of the phospholipids facing into the interior of the
membrane and the hydrophilic head groups on the outside. The most common lipids in
most cell membranes are the phospholipids. The head group of a glycolipid is composed
of sugars.
11-2 $e%
11-3 $c% The remaining answers are false. &hospholipids form bilayers only in polar
sol!ents. Nuclei and mitochondria are enclosed by to membranes. Membrane
lipids rarely flip-flop between one monolayer and the other. The preferred form
of a lipid bilayer in water is a closed sphere, so that the hydrophobic groups at
the edges of the bilayer can a!oid contact with water.

11-4 (hoice $b% is the correct answer. t colder temperatures, the membrane will be less fluid.
Bence, in order to maintain the status .uo, the bacterium will ha!e to take measures to
increase membrane fluidity. ,ncreasing the length of the hydrocarbon tails $choice $a%%
would decrease membrane fluidity, while decreasing the number of glycolipids $choice
$e%% would ha!e little or no effect. 1ecreasing the proportion of fatty acid tails with no
double bonds $fully saturated% $choice $c%% would decrease membrane fluidity. <acteria
do not ha!e cholesterol $choice $d%%.
11-5 $a% *nsaturated fatty acid tails do ha!e fewer hydrogen atoms and do interact less
well with one another but not for the reason stated. The decrease in interaction is
due to a decrease in !an der "aals interactions between the hydrocarbon tails
because they can pack less closely. Bydrocarbon chains cannot form hydrogen
bonds with each other.
11-6 $d%
11-7 $c% s phospholipids are initially inserted into the cytosolic face of the lipid bilayer,
flippases are re.uired to mo!e 3 and 4 to the opposite face, as they cannot
spontaneously flip across the bilayer.
11-8 $b%
1)4
11-9 . 'ee Figure 77-;.
Figure 77-;
<., (. 'ee Figure 77-;<.
Figure 77-;<
11-10 $c%
11-11 $a% The peptide is e/tremely hydrophilic and is, therefore, unlikely to be inserted into
the lipid bilayer. ,t is also too short to span the membrane as an -heli/. lthough
it is possible that the lysines interact with an acidic membrane protein, if such an
interaction were solely responsible for attaching the protein to the membrane, it
would not re.uire a detergent to remo!e the protein, since ionic interactions are
disrupted by milder treatments such as salt washes and pB changes.
11-12 (hoice $b% is the correct answer. ,nsertion of a pore-forming protein into the lipid bilayer
will ha!e the effects noted by making the red blood cell unable to regulate its internal ion
composition. The type of protein most likely to form the sort of nonspecific pore
described is a -barrel protein. +nabling membrane lipids to flip from one layer of the
bilayer to the other should not affect permeability $choice $a%%. protease would ha!e no
effect on liposomes made of pure phospholipids $choice $c%%. &roteins containing a single
hydrophobic -heli/ would not form a channel through the membrane $choice $d%%.
ddition of carbohydrate groups to lipids should not make the bilayer any more
permeable to ions $choice $e%%.
1)$
11-13 There are se!eral ways that membrane proteins can associate with the cell membrane.
Membrane proteins that e/tend through the lipid bilayer are called transmembrane
proteins and ha!e hydrophobic regions that are e/posed to the interior of the bilayer. :n
the other hand, membrane-associated proteins do not span the bilayer and instead
associate with the membrane through an -heli/ that is amphipathic. :ther proteins are
co!alently attached to lipid molecules that are inserted in the membrane. "eripheral
membrane proteins are linked to the membrane through nonco!alent interactions with
other membrane-bound proteins.
11-14 (hoice $e% is the correct answer. ,n transmembrane proteins that form an a.ueous pore
through the membrane, the pore is lined with hydrophilic amino acid side chains. The
other statements are all true. ,ntegral membrane proteins often precipitate in a.ueous
solutions because of their stretches of hydrophobic amino acids $choice $a%%. &roteins
also contain hydrophobic amino acids in parts of the protein other than the membrane-
spanning region, for e/ample, in the cores of their e/tracellular or cytoplasmic domains
$choice $b%%. &eripheral membrane proteins are attached to the membrane by nonco!alent
interactions with other membrane proteins, making their membrane association relati!ely
weak and thus disruptable by gentle detergents $choice $c%%.
11-15 (hoice $a% is the correct answer. "hen an -heli/ tra!erses a lipid bilayer, the amino acid
side chains are e/posed to the hydrophobic portion of the lipid bilayer and thus should
consist of nonpolar side chains. The se.uence gi!en in choice $a% contains nonpolar
amino acids. (hoices $b% and $c% are inappropriate, as they both contain se!eral
negati!ely and positi!ely charged amino acids.
$Note that in addition, choice $b% contains two prolines, which would render this
se.uence unable to form an -helical structure and therefore lead to e/posure of the
hydrogen-bonding moieties in the polypeptide background to the nonpolar en!ironment
of the lipid bilayer.%
11-16 $a% ,n a -sheet, the amino acid side chains pro0ect alternately abo!e and below the
plane of the sheet. Therefore, e!ery other amino acid side chain will face the
same side of the strand. ,f a -sheet were part of a -barrel pore, that would mean
that one side of the sheet would face the lipid bilayer while the other side would
face the hydrophilic pore. This would necessitate an alternation between
hydrophilic and hydrophobic amino acid side chains so that one side of the sheet
would be hydrophobic while the other side was hydrophilic. The amino acids in
choice $a% alternate between amino acids with nonpolar $hydrophobic% side chains
and amino acids with polar $hydrophilic% side chains.
11-17 $b%, $d%, and $e%
1)%
11-18 $a%, $d% The results from the e/tracts of normal cells show that protein is an integral
protein that remains in the membrane through all the treatments, while protein <
is a peripheral protein that can be remo!ed from the membrane by urea. ,n the cell
e/tracts from the mutants in , the protein still remains in the membrane, but
the < protein does not. This is consistent with the mutation in affecting its
interaction with <. The same results are obtained when the < protein is mutant,
which is consistent with the idea that and < interact. The loss of an interaction
between an integral membrane protein and a protein in the corte/ would be more
likely to result in a change in cell shape than the loss of an interaction between an
integral membrane protein and a protein on the e/terior of the cell.
11-19 detergent has one hydrophobic tail while a phospholipid has two hydrophobic tails.
This difference is reflected in the geometry of the molecules, with detergent molecules
being shaped more like cones whereas phospholipids are more cylindrical. The cone-like
detergent molecules will aggregate into micelles, with the hydrophilic head group on the
outside and the hydrophobic tail group on the inside. :n the other hand, the cylindrical
shape of a phospholipid means that when phospholipids aggregate, the formation of a
bilayer is most energetically fa!orable, with the hydrophobic tails on the inside of the
two-layered sheet and the hydrophilic heads facing the water molecules. Bowe!er, it is
not energetically fa!orable for a phospholipid bilayer to e/ist as a sheet, because the
e/posed free edges would lead to e/posure of the hydrophobic tails to water. Therefore,
phospholipid bilayers spontaneously close to form spherical liposomes.
11-20 $e%
11-21 $c% The sugars in an oligosaccharide side chain attached to the cell surface can be
0oined together in many different ways and in !aried se.uences.
11-22 ny combination of these four answers is acceptable=
7. The protein can be attached to the cell corte/ inside the cell.
?. The protein can be attached to the e/tracellular matri/ outside the cell.
D. The protein can be attached to other proteins on the surface of a different cell.
E. The protein can be restricted in its ability to diffuse by a diffusion barrier, such as
that set up by specialized 0unctional proteins at a tight 0unction.
11-23 . 3 diffuses the fastest, followed by 5, with 4 barely diffusing at all. $The faster
the reco!ery of fluorescence in the bleached area, the greater the diffusion
coefficient of the protein and the faster the protein diffuses.%
<. ,t is unlikely that 3 and 5 are part of the same protein comple/ because then the
rate of diffusion of 3 and 5 should be the same.
1)#
11-24 . &rotein ( displays the least amount of motion and therefore is the one most likely
to be tethered to the cytoskeleton.
<. The fluidity of the lipid bilayer should not be affected by the anchoring of
membrane proteins. The lipid molecules should still be able to flow around
anchored proteins much like water flows around rocks in a stream. $Note that the
fluidity of the lipid bilayer is affected by the degree of saturation found in the
hydrocarbon tails, the length of the hydrocarbon tails, and in animal cells, the
amount of cholesterol in the membrane.%
1))