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Mamu
Mamu
Mamu
endoplasmic lysosome
reticulum
Golgi
transport apparatus
vesicle
plasma
membrane
mitochondrion
3 Membrane Functions
1 receiving
information
2 import and
export of
small molecules 1. Compartmentalization
4. Transport of Solutes
It facilitates transport of solutes from one side of membrane to another e.g. sugar amino acids,
ions.
5. Signal Transduction
Membrane possess receptors to which various ligands can bind to generate a signal that
stimulates or inhibits internal activities.
6. Cell to cell interaction 7. Energy transduction
4 What are membranes made up of?
Membrane protein content is highly variable. The amount of proteins equals or exceeds the quantity of lipid in nearly all membranes. The
outstanding exception is myelin, an electri-cal insulator found on many nerve fibers.
Cell Membrane
consists of
functions as
whose functions include
Selective barrier between cytosol
and external environment Structural stability Cell recognition Immune response
5 The Fluid Mosaic Model
Phospholipid
bilayer
Peripheral membrane Cholesterol molecules interspersed Some membrane Some integral proteins
proteins do not penetrate among phospholipid tails in the proteins interact with the cross the entire phospholipid
Inside of cell the bilayer at all. bilayer influence the fluidity of interior cytoskeleton. bilayer; others penetrate only
fatty acids in the membrane. partially into the bilayer.
6.1 The Fluid Mosaic Model The general molecular structure of bio-
logical membranes is a continuous phospholipid bilayer which has pro-
teins embedded in or associated with it.
CH3
HC CH3
CH3
CH3
2-methylpropane
HC CH3
Figure 11–9 A hydrophobic molecule
CH3 tends to avoid water. Because the
_ 2-methylpropane molecule is entirely
δ hydrophobic, it cannot form favorable
O
H H interactions with water. This causes the
δ+ δ+ adjacent water molecules to reorganize into
a cagelike structure around it, to maximize
water 2-methylpropane in water their hydrogen bonds with each other.
QUESTION 11–1
Water molecules are said “to reorganize into a cagelike structure” around hydrophobic compounds
(e.g., see Figure 11–9). This seems paradoxical because water molecules do not interact with the hydrophobic
compound. So how could they “know” about its presence and change their behavior to interact differently with
one another? Discuss this argument and, in doing so, develop a clear concept of what is meant by a “cagelike”
structure. How does it compare to ice? Why would this cagelike structure be energetically unfavorable?
ANSWER 11–1 Water is a liquid, and the hydrogen bonds that form between water molecules are not static;
they are continually broken and remade again by thermal motion. When a water molecule happens to be next
to a hydrophobic molecule, it is more restricted in motion and has fewer neighbors with which it can interact,
because it cannot form any hydrogen bonds in the direction of the hydrophobic molecule. It will therefore form
hydrogen bonds to the more limited number of water molecules in its proximity. Bonding to fewer partners
results in a more ordered water structure, which represents the cagelike structure in Figure 11–9. This structure
has been likened to ice, although it is a more transient, less organized, and less extensive network than even a
tiny ice crystal. The formation of any ordered structure decreases the entropy of the system and is thus
energetically unfavorable (discussed in Chapter 3).
(A) (B)
Nonpolar
molecule Nonpolar
molecule
Nonpolar
molecule
Nonpolar
molecule Figure 2.9 The hydrophobic effect. the
aggregation of nonpolar groups in water
leads to an increase in entropy owing to the
release of water molecules into bulk water.
Consider the introduction of a single nonpolar molecule, such as benzene, into some water (Figure 2.9).
A cavity in the water is created because the benzene has no chemical means of interacting with the water molecule.
The cavity temporarily disrupts some hydrogen bonds between water molecules. The displaced water molecules then
reorient themselves to form the maximum number of new hydrogen bonds. How-ever, there are many fewer ways of forming
hydrogen bonds around the benzene molecule than there are in pure water. The water molecules around the benzene
molecule are much more ordered than elsewhere in the solution. The introduction of the nonpolar molecule into water has
resulted in a decrease in the entropy of water. Now consider the arrangement of two benzene molecules in water. They do
not reside in separate small cavities (Figure 2.9A); instead, they coalesce into a single larger one (Figure 2.9B). They become
organized. The energetic basis for the formation of this order is that the association of the benzene molecules re-leases
some of the ordered water molecules around the separated benzenes, in-creasing the entropy of the system. Nonpolar
solute molecules are driven together in water not primarily because they have a high affinity for each other but because, when
they do associate, they release water molecules. This entropy-driven associa-tion is called the hydrophobic effect, and the
resulting interactions are called hy-drophobic interactions. Hydrophobic interactions form spontaneously—no input of
energy is required—because, when they form, the entropy of water increases.
ENERGETICALLY UNFAVORABLE
The same forces that drive the amphipathic molecules to form a bilayer
in a planar phospholipid bilayer, help to make the bilayer self-sealing. Any tear in the sheet will create a
hydrophobic tails (white layer) free edge that is exposed to water. Because this situation is energetically
are exposed to water along
the edges unfavorable, the molecules of the bilayer will spontaneously rearrange
to eliminate the free edge. If the tear is small, this spontaneous re-
arrangement will exclude the water molecules and lead to repair of the
bilayer, restoring a single continuous sheet. If the tear is large, the sheet
may begin to fold in on itself and break up into separate closed vesi-
cles. In either case, the overriding principle is that free edges are quickly
eliminated.
formation of a sealed The prohibition on free edges has a profound consequence: the only way
compartment shields
hydrophobic tails from an amphipathic sheet can avoid having free edges is to bend and seal,
water forming a boundary around a closed space (Figure 11–12). Therefore,
amphipathic molecules such as phospholipids necessarily assemble into
self-sealing containers that define closed compartments—from vesicles
ENERGETICALLY FAVORABLE and organelles to entire cells. This remarkable behavior, fundamental to
the creation of a living cell, is essentially a by-product of the nature of
Figure 11–12 Phospholipid bilayers membrane lipids: hydrophilic at one end and hydrophobic at the other.
spontaneously close in on themselves to
form sealed compartments. The closed
structure is stable because it avoids the
exposure of the hydrophobic hydrocarbon
tails to water, which would be energetically
unfavorable.
lateral diffusion
flip-flop
(rarely occurs)
7 The Lipid Bilayer Is a Flexible Two-dimensional Fluid
flexion rotation
Figure 11–14 Membrane phospholipids Phospholipid molecules very rarely tumble from one half of the bilayer,
move within the lipid bilayer. Because of or monolayer, to the other. Without proteins to facilitate the process, it
these motions, the bilayer behaves as a two- is estimated that this event, called “flip-flop,” occurs less than once a
dimensional fluid, in which the individual month for any individual lipid molecule under conditions similar to
lipid molecules are able to move in their
own monolayer. Note that lipid molecules those in a cell. On the other hand, as the result of random thermal
do not move spontaneously from one motions, lipid molecules continuously exchange places with their
monolayer to the other. neighbors within the same monolayer. This exchange leads to rapid
lateral diffusion of lipid molecules within the plane of each
monolayer.
Individual lipid molecules not only flex their hydrocarbon tails, but they
also rotate rapidly about their long axis—some reaching speeds of
500 revolutions per second. .
CH2 N+(CH3)3
CH2 8 The Fluidity of a Lipid Bilayer Depends on Its
O
_
Composition
O P O
O The fluidity of a cell membrane—the ease with which its lipid molecules move within the
CH2 CH CH2 plane of the bilayer—is important for membrane func-tion and has to be maintained within
O O certain limits. Just how fluid a lipid bilayer is at a given temperature depends on its
C O C O phospholipid composi-tion and, in particular, on the nature of the hydrocarbon tails: the
CH2 CH2
closer and more regular the packing of the tails, the more viscous and less fluid the bilayer
CH2 CH2
will be.
CH2 CH2
CH2 CH2 Two major properties of hydrocarbon tails affect how tightly they pack in the bilayer: their
CH2 CH2 length and the number of double bonds they con-tain. A shorter chain length reduces the
CH2 CH2 tendency of the hydrocarbon tails to interact with one another and therefore increases the
CH2 CH2 fluidity of the bilayer.
CH2 CH double
CH2 CH
bond Each double bond in an unsaturated tail creates a small kink in the tail, which makes it
CH2 CH2 more difficult for the tails to pack against one another. For this reason, lipid bilayers that
CH2
CH2 contain a large proportion of unsaturated hydrocarbon tails are more fluid than those with
CH2
CH2
CH2
lower proportions.
CH2 CH2
CH2 CH2
In animal cells, membrane fluidity is modulated by the inclusion of the
CH2 CH2 sterol cholesterol. This molecule is present in especially large amounts
CH2
CH3 in the plasma membrane, where it constitutes approximately 20% of the
CH3 lipids in the membrane by weight. With its short and rigid steroid ring
structure, cholesterol can fill the spaces between neighboring phospho-
lipid molecules left by the kinks in their unsaturated hydrocarbon tails
(Figure 11–15). In this way, cholesterol tends to stiffen the bilayer, mak-
ing it less flexible, as well as less permeable.
CYTOSOL
X Y
NH2
P P
EXTRACELLULAR SPACE
lipid
bilayer
CYTOSOL
COOH
Figure 11–21 Membrane proteins can associate with the lipid bilayer in different ways. (A) Transmembrane
proteins can extend across the bilayer as a single α helix, as multiple α helices, or as a rolled-up β sheet (called a
β barrel). (B) Some membrane proteins are anchored to the cytosolic half of the lipid bilayer by an amphipathic
α helix. (C) Others are linked to either side of the bilayer solely by a covalently attached lipid molecule (red zigzag
lines). (D) Many proteins are attached to the membrane only by relatively weak, noncovalent interactions with other
membrane proteins. (A−C) are examples of integral membrane proteins; the proteins shown in (D) are considered
peripheral membrane proteins.
Although the lipid bilayer has a uniform structure, proteins can interact
with a cell membrane in a number of different ways.
• Many membrane proteins extend through the bilayer, with part of
their mass on either side (Figure 11–21A). Like their lipid neighbors,
these transmembrane proteins are amphipathic, having both
hydrophobic and hydrophilic regions. Their hydrophobic regions lie
in the interior of the bilayer, nestled against the hydrophobic tails
of the lipid molecules. Their hydrophilic regions are exposed to the
aqueous environment on either side of the membrane.
• Other membrane proteins are located almost entirely in the cytosol
and are associated with the cytosolic half of the lipid bilayer by an
amphipathic α helix exposed on the surface of the protein (Figure
11–21B).
• Some proteins lie entirely outside the bilayer, on one side or the
other, attached to the membrane by one or more covalently attached
lipid groups (Figure 11–21C).
• Yet other proteins are bound indirectly to one face of the membrane
or the other, held in place only by their interactions with other
membrane proteins (Figure 11–21D).
Proteins that are directly attached to the lipid bilayer—whether they are
transmembrane, associated with the lipid monolayer, or lipid-linked—can
be removed only by disrupting the bilayer with detergents, as discussed
shortly. Such proteins are known as integral membrane proteins. The
remaining membrane proteins are classified as peripheral membrane pro-
teins; they can be released from the membrane by more gentle extraction
procedures that interfere with protein–protein interactions but leave the
lipid bilayer intact.