Membrane Structure.

The structure and function of the plasma membrane.

Membrane Proteins.
Association of Membrane Proteins with the Lipid Bilayer.
Membrane Structure

A living cell is a self-reproducing system of molecules held inside a

container.
That container is the plasma membrane—a protein-studded, fatty
film so thin that it cannot be seen directly in the light microscope.
Every cell on Earth uses such a membrane to separate and protect
its chemical components from the outside environment.
Without membranes, there would be no cells, and thus no life.
 The structure of the plasma
membrane is simple: it consists of a
two-ply sheet of lipid molecules about
5 nm—or 50 atoms—thick, into which
proteins have been inserted.
 Its properties, however, are unlike
those of any sheet of material we are
familiar with in the everyday world. Figure 11–1 Cell membranes act as
 Although it serves as a barrier to selective barriers. The plasma membrane
separates a cell from its surroundings, enabling the molecular
prevent the contents of the cell from composition of a cell to differ from that of its environment.
(A) In some bacteria, the plasma membrane
escaping and mixing with molecules in is the only membrane.
the surrounding environment (Figure (B) In addition to a plasma membrane, eukaryotic cells also have
internal membranes that enclose individual organelles. All cell
11−1), the plasma membrane does membranes prevent molecules on one side from freely mixing
with those on the other, as indicated schematically by the colored
much more than that. dots.
 If a cell is to survive and grow, nutrients
must pass inward across the plasma
membrane, and waste products must
make their way out.
 To facilitate this exchange, the membrane
is penetrated by highly selective channels
and transporters—proteins that allow
specific, small molecules and ions to be
imported and exported. Figure 11–1 Cell membranes act as
selective barriers. The plasma membrane separates a cell from its
As shown in Figure 11–1, many surroundings, enabling the molecular composition of a
cell to differ from that of its environment.
bacteria have only a single membrane (A) In some bacteria, the plasma membrane
the plasma membrane—whereas is the only membrane.
(B) In addition to a plasma membrane, eukaryotic cells also have
eukaryotic cells also contain internal internal membranes that enclose individual organelles. All cell
membranes prevent molecules on one side from freely
membranes that enclose intracellular mixing with those on the other, as indicated schematically by the
colored dots.
compartments.
Other proteins in the membrane act as sensors,
or receptors, that enable the cell to receive
information about changes in its environment
and respond to them in appropriate ways.
The mechanical properties of the plasma
membrane are equally impressive. When a
cell grows, so does its membrane: this
remarkable structure enlarges in area by adding
new membrane without ever losing its
continuity, and it can deform without tearing,
allowing the cell to move or change shape
(Figure 11−2). Figure 11–2 The plasma membrane is involved in cell
The membrane is also self-healing: if it is communication, import and export of molecules, and cell growth
and motility.
pierced, it neither collapses like a balloon nor (1) Receptor proteins in the plasma membrane enable
remains torn; instead, the membrane quickly the cell to receive signals from the environment;
reseals. (2) channels and transporters in the membrane enable the import and
export of small molecules;
(3) the flexibility of the membrane and its capacity for
expansion allow the cell to grow, change shape, and move.
Receptor proteins can be classified by their location.
Transmembrane receptors include ligand-gated ion channels, G
protein-coupled receptors, and enzyme-linked hormone receptors.
Intracellular receptors are those found inside the cell, and include
cytoplasmic receptors and nuclear receptors.
A molecule that binds to a receptor is called a ligand and can be a
protein, peptide (short protein), or another small molecule, such as
a neurotransmitter, hormone, pharmaceutical drug, toxin, calcium
ion or parts of the outside of a virus or microbe.
The internal membranes form various
organelles, including the endoplasmic
reticulum, Golgi apparatus, endosomes,
and mitochondria (Figure 11–3).
Although these internal membranes are
constructed on the same principles as the
plasma membrane, they differ subtly in
composition, especially in their resident
proteins.

Figure 11–3 Internal membranes form many different compartments

in a eukaryotic cell. Some of the main membrane-enclosed organelles
in a typical animal cell are shown here.
Note that the nucleus and mitochondria are each
enclosed by two membranes.
Regardless of their location, all cell
membranes are composed of lipids
and proteins and share a common
general structure (Figure 11–4).
The lipids are arranged in two
closely apposed sheets, forming a
lipid bilayer. This lipid bilayer serves
as a permeability barrier to most
water-soluble molecules, while the
proteins embedded within it carry
out the other functions of the
membrane and give different
membranes their individual Figure 11–4 A cell membrane consists of a lipid bilayer in which proteins
are embedded. (A) An electron micrograph of a plasma membrane of a
characteristics. The functions of cell human red blood cell seen in cross section. In this image, the proteins
membranes, including their role in that extend from either side of the bilayer form the two closely spaced
cell communication, the transport dark lines indicated by the brackets; the thin, white layer between them
is the lipid bilayer. (B) Schematic drawing showing a three dimensional
of small molecules, and energy view of a cell membrane. (A, by permission of E.L. Bearer.)
generation.
FIGURE 4-10
Cell membranes are made of a phospholipid bilayer.
Each phospholipid molecule has a polar “head” and a
two-part nonpolar “tail.”
Membrane Lipids Form Bilayers in Water

The lipids found in cell membranes

combine two very different properties in a
single molecule: each lipid has a
hydrophilic (“water-loving”) head and a
hydrophobic (“water-fearing”) tail.

The most abundant lipids in cell

membranes are the phospholipids, which
have a phosphate-containing, hydrophilic
head linked to a pair of hydrophobic, Figure 11–5 Cell membranes are packed
with phospholipids. A typical membrane
hydrocarbon tails (Figure 11–5). phospholipid molecule has a hydrophilic
head and two hydrophobic tails.
 For example, phosphatidylcholine, one of the
most abundant phospholipids in the
membranes of animals and plants, has the
small molecule choline attached to a
phosphate group as its hydrophilic head (Figure
11–6).
Figure 11–6 Phosphatidylcholine is the most common
phospholipid in cell membranes. It is represented
schematically in (A), as a chemical formula in (B), as a
space-filling model in (C), and as a symbol in (D). This
particular phospholipid is built from five parts: the
hydrophilic head, which consists of choline linked to a
phosphate group;
two hydrocarbon chains, which form the hydrophobic
tails; and a molecule of glycerol, which links the head
to the tails. Each of the hydrophobic tails is a fatty acid
—a hydrocarbon chain with a carboxyl (–COOH)
group at one end; glycerol attaches via this carboxyl
group, as shown in (B). A kink in one of the
hydrocarbon chains occurs where there is a double
bond between two carbon atoms. (The “phosphatidyl”
part of the name of a phospholipid refers to the
phosphate–glycerol–fatty acid portion of the
molecule.)
 Figure 11–7 Different types of membrane
lipids are all amphipathic. Each of the
three types shown here has a hydrophilic
head and one or two hydrophobic tails.
The hydrophilic head is serine phosphate
(shaded blue and yellow) in
phosphatidylserine, an –OH group (blue)
in cholesterol, and the sugar galactose
plus an –OH group (both blue) in
galactocerebroside.

Phospholipids are not the only membrane lipids that

are amphipathic, a term used to describe molecules
with both hydrophilic and hydrophobic parts.
Cholesterol, which is found in animal cell membranes,
and glycolipids, which have sugars as part of their
hydrophilic head, are also amphipathic (Figure 11–7).
Having both hydrophilic and hydrophobic parts
plays a crucial part in driving lipid molecules to
assemble into bilayers in an aqueous
environment.
Hydrophilic molecules dissolve readily
in water because they contain either
charged groups or uncharged polar
groups that can form electrostatic
attractions or hydrogen bonds with
water molecules (Figure 11–8).
Hydrophobic molecules, by contrast,
are insoluble in water because all—or
almost all—of their atoms are
uncharged and nonpolar; they
therefore cannot form favorable
interactions with water molecules.
The Lipid Bilayer Is a
Flexible Two-dimensional
Fluid
The lipid bilayer therefore
behaves as a two dimensional
fluid, a fact that is crucial for
membrane function and
integrity.
At the same time, the lipid
bilayer is also flexible—that is,
it is able to bend.
Like fluidity, flexibility is
important for membrane
function, and it sets a lower Figure 11–11 Amphipathic phospholipids form a bilayer in water.
(A) Schematic drawing of a phospholipid bilayer in water.
limit of about 25 nm to the (B) Computer simulation showing the phospholipid molecules (red heads and
vesicle diameter that cell orange tails) and the surrounding water molecules
membranes can form. (blue) in a cross section of a lipid bilayer. (B, adapted from R.M. Venable et al.,
Science 262:223–228, 1993.)
Using such simple synthetic bilayers, investigators can measure the
movements of the lipid molecules in a lipid bilayer.
These measurements reveal that some types of movement are rare, while
others are frequent and rapid.
Thus, in synthetic lipid bilayers, phospholipid molecules very rarely tumble
from one half of the bilayer, or monolayer, to the other.
Without proteins to facilitate the process, it is estimated that this event, called
“flip-flop,” occurs less than once a month for any individual lipid molecule
under conditions similar to those in a cell.
On the other hand, as the result of random thermal motions, lipid molecules
continuously exchange places with their neighbors within the same
monolayer.

This exchange leads to rapid lateral diffusion of lipid molecules within the
plane of each monolayer, so that, for example, a lipid in an artificial bilayer
may diffuse a length equal to that of an entire bacterial cell (~2 μm) in about
one second.
Similar studies show that 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.
Studies of whole cells—and of isolated cell membranes—indicate
that lipid molecules in cell membranes undergo the same
movements as they do in synthetic bilayers.
The Fluidity of a Lipid Bilayer Depends on Its Composition

The fluidity of a cell membrane—the ease with which its lipid

molecules move within the plane of the bilayer—is important for
membrane function and has to be maintained within certain limits.
Just how fluid a lipid bilayer is at a given temperature depends on
its phospholipid composition and, in particular, on the nature of
the hydrocarbon tails: the closer and more regular the packing of
the tails, the more viscous and less fluid the bilayer will be.
Two major properties of hydrocarbon tails affect how tightly they
pack in the bilayer:
their length and
the number of double bonds they contain.
A shorter chain length reduces the tendency of the hydrocarbon
tails to interact with one another and therefore increases the
fluidity of the bilayer.
The hydrocarbon tails of membrane phospholipids vary in
length between 14 and 24 carbon atoms, with 18 or 20 atoms
being the most common.
For most phospholipids, one of these hydrocarbon tails
contains only single bonds between its adjacent carbon atoms,
whereas the other tail includes one or more double bonds.
The chain that harbors a double bond does not contain the
maximum number of hydrogen atoms that could, in principle, be
attached to its carbon backbone; it is thus said to be unsaturated
with respect to hydrogen.
The hydrocarbon tail with no double bonds has a full complement
of hydrogen atoms and is said to be saturated.
Each double bond in an unsaturated tail creates a small kink in the
tail, which makes it more difficult for the tails to pack against one
another.
For this reason, lipid bilayers that contain a large proportion of
unsaturated hydrocarbon tails are more fluid than those with
lower proportions.
In animal cells, membrane fluidity is modulated by the inclusion
of the sterol cholesterol.
This molecule is present in especially large amounts in the plasma
membrane, where it constitutes approximately 20% of the
lipids in the membrane by weight.
With its short and rigid steroid ring structure, cholesterol can fill
the spaces between neighboring phospholipid molecules left by
the kinks in their unsaturated hydrocarbon tails.
In this way, cholesterol tends to stiffen the bilayer, making
it less flexible, as well as less permeable.
For all cells, membrane fluidity is important for a number of
reasons.
It enables many membrane proteins to diffuse rapidly in the plane
of the bilayer and to interact with one another, as is crucial, for
example, in cell signaling. (Cell signaling is also intimately involved
in the regulation of cell growth and division.)
It permits membrane lipids and proteins to diffuse from sites where
they are inserted into the bilayer after their synthesis to other
regions of the cell.
It ensures that membrane molecules are distributed evenly
between daughter cells when a cell divides.
And, under appropriate conditions, it allows membranes to fuse
with one another and mix their molecules.
Certain Phospholipids Are Confined to One Side of the
Membrane

Most cell membranes are asymmetric: the two halves of the bilayer
often include strikingly different sets of phospholipids.
But if membranes emerge from the ER with an evenly assorted set of
phospholipids, where does this asymmetry arise?
It begins in the Golgi apparatus.
The Golgi membrane contains another family of phospholipid-
handling transporters, called flippases.
The action of these flippases—and of similar transporters in the
plasma membrane—initiates and maintains the asymmetric
arrangement of phospholipids that is characteristic of the
membranes of animal cells.
This asymmetry is preserved as membranes bud from one
organelle and fuse with another—or with the plasma
membrane. This means that all cell membranes have
distinct “inside” and “outside” faces: the cytosolic
monolayer always faces the cytosol, while the noncytosolic
monolayer is exposed to either the cell exterior—in the
case of the plasma membrane— or the interior space
(lumen) of an organelle.
This conservation of orientation applies not only to the
phospholipids that make up the membrane, but also to any
proteins that might be inserted in the membrane (Figure
11–18). This positioning is very important, as a protein’s
orientation within the lipid bilayer is crucial for its function.
Figure 11–18 Membranes retain their orientation during transfer between cell compartments. Membranes are transported by a
process of vesicle budding and fusing. Here, a vesicle is shown budding from the Golgi apparatus and fusing with the plasma membrane.
Note that the orientations of both the membrane lipids and proteins are preserved during the process: the original cytosolic surface of the
lipid bilayer (pink ) remains facing the cytosol, and the noncytosolic surface (red ) continues to face away from the cytosol, toward the
lumen of the Golgi and the transport vesicle—or toward the extracellular fluid. Similarly, the glycoprotein shown here (blue and green)
remains in the same orientation, with its attached sugar facing the noncytosolic side.
 Among lipids, those that show the most dramatically
lopsided distribution in cell membranes are the glycolipids,
which are located mainly in the plasma membrane, and only
in the noncytosolic half of the bilayer (Figure 11–19).
The sugar groups of these membrane lipids face the cell
exterior, where they form part of a continuous coat of
carbohydrate that surrounds and protects animal cells.
Glycolipid molecules acquire their sugar groups in the Golgi
apparatus, where the enzymes that engineer this chemical
modification are confined.
These enzymes are oriented such that sugars are added only
to lipid molecules in the noncytosolic half of the bilayer.

Figure 11–19 Phospholipids and glycolipids are distributed asymmetrically in the lipid bilayer of an animal cell
plasma membrane. Phosphatidylcholine (red ) and sphingomyelin (brown) are concentrated in the noncytosolic
monolayer, whereas phosphatidylserine (light green) and phosphatidylethanolamine (yellow) are found mainly on
the cytosolic side. In addition to these phospholipids, phosphatidylinositols (dark green head group), a minor
constituent of the plasma membrane, are shown in the cytosolic monolayer, where they participate in cell signaling.
Glycolipids are drawn with hexagonal blue head groups to represent sugars; these are found exclusively in the
noncytosolic monolayer of the membrane. Within the bilayer, cholesterol (green) is distributed almost equally in
both monolayers.
 Once a glycolipid molecule has been created in this way, it
remains trapped in this monolayer, as there are no flippases
that transfer glycolipids to the cytosolic side. Thus, when a
glycolipid molecule is finally delivered to the plasma
membrane, it displays its sugars to the exterior of the cell.
Other lipid molecules show different types of asymmetric
distributions, which relate to their specific functions.
For example, the inositol phospholipids— a minor component
of the plasma membrane—have a special role in relaying
signals from the cell surface into the cell interior; thus they are
concentrated in the cytosolic half of the lipid bilayer.

Figure 11–19 Phospholipids and glycolipids are distributed asymmetrically in the lipid bilayer of an animal cell
plasma membrane. Phosphatidylcholine (red ) and sphingomyelin (brown) are concentrated in the noncytosolic
monolayer, whereas phosphatidylserine (light green) and phosphatidylethanolamine (yellow) are found mainly on
the cytosolic side. In addition to these phospholipids, phosphatidylinositols (dark green head group), a minor
constituent of the plasma membrane, are shown in the cytosolic monolayer, where they participate in cell signaling.
Glycolipids are drawn with hexagonal blue head groups to represent sugars; these are found exclusively in the
noncytosolic monolayer of the membrane. Within the bilayer, cholesterol (green) is distributed almost equally in
both monolayers.
Fluid Mosaic Model
A cell’s plasma membrane is
surprisingly dynamic.
Scientists describe the cell
membrane as a fluid mosaic.
The fluid mosaic model states
that the phospholipid bilayer
behaves like a fluid more than
it behaves like a solid.
The membrane’s lipids and
proteins can move laterally
within the bilayer. As a result
of such lateral movement, the
pattern, or “mosaic,” of lipids
and proteins in the cell
membrane constantly changes.
What does fluid mosaic model mean?

The fluid mosaic model describes the cell membrane as

a tapestry of several types of molecules (phospholipids,
cholesterols, and proteins) that are constantly moving.
This movement helps the cell membrane maintain its role
as a barrier between the inside and outside of the cell
environments.
What is an important function of the fluid mosaic model?

The fluid mosaic model is the most acceptable model of

the plasma membrane.
Its main function is to separate the contents of the cell from the outside.

Who gave fluid mosaic model?

In 1972 the Fluid—Mosaic Membrane Model of membrane structure was

proposed based on thermodynamic principals of organization of membrane
lipids and proteins and available evidence of asymmetry and lateral mobility
within the membrane matrix [S. J. Singer and G. L. Nicolson.
MEMBRANE PROTEINS

Although the lipid bilayer provides the basic structure of all cell
membranes and serves as a permeability barrier to the
hydrophilic molecules on either side of it, most membrane
functions are carried out by membrane proteins.
In animals, proteins constitute about 50% of the mass
of most plasma membranes, the remainder being lipid plus the
relatively small amounts of carbohydrate found on some of the
lipids (glycolipids) and many of the proteins (glycoproteins).
Because lipid molecules are much smaller than proteins, however,
a cell membrane typically contains about 50 times the number of
lipid molecules compared to protein molecules.
Membrane proteins serve many functions.
Some transport particular nutrients, metabolites, and ions across
the lipid bilayer.
Others anchor the membrane to macromolecules on either side.
Still others function as receptors that detect chemical signals in the
cell’s environment and relay them into the cell interior, or work as
enzymes to catalyze specific reactions at the membrane (Figure
11–20 and Table 11–1).
Each type of
cell membrane contains
a different set of
proteins, reflecting the
specialized
functions of the
particular membrane.
In this section, we
discuss the structure of
membrane proteins and
how they associate with
the lipid bilayer.
Membrane Proteins
Associate with the Lipid
Bilayer in Different Ways

Although the lipid

bilayer has a uniform
structure, proteins can
interact with a cell
membrane in a number
of different ways.

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.
• 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 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
hydrophilic regions are
rolled-up β sheet (called a β barrel). (B) Some membrane proteins are anchored to the cytosolic half of
exposed to the aqueous the lipid bilayer by an amphipathic α helix. (C) Others are linked to either side of the bilayer solely by
environment on either a covalently attached lipid molecule (red zigzag
side of the membrane. 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.
• 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
Figure 11–21 Membrane proteins can associate with the lipid bilayer in different ways. (A)
bilayer, on one side or Transmembrane proteins can extend across the bilayer as a single α helix, as multiple α helices, or
the other, attached to 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
the membrane by one solely by a covalently attached lipid molecule (red zigzag lines). (D) Many proteins are attached to
or more covalently 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
attached lipid groups peripheral membrane proteins.
• 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 Figure 11–21 Membrane proteins can associate with the lipid bilayer in different ways. (A)
—can be removed only by 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
disrupting the bilayer with half of the lipid bilayer by an amphipathic α helix. (C) Others are linked to either side of the bilayer
detergents, as discussed 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.
shortly. (A−C) are examples of integral membrane proteins; the proteins shown in (D) are considered
peripheral membrane proteins.
Such proteins are
known as integral
membrane proteins.
The remaining
membrane proteins
are classified as
peripheral membrane
proteins; they can be
released from the
membrane by more
gentle extraction
procedures that
interfere with protein– Figure 11–21 Membrane proteins can associate with the lipid bilayer in different ways. (A)
protein interactions 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
but leave the lipid half of the lipid bilayer by an amphipathic α helix. (C) Others are linked to either side of the bilayer
bilayer intact. 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.
The cell membranes of eukaryotes also contain lipids, called
sterols, between the tails of the phospholipids.
The major membrane sterol in animal cells is cholesterol.
Sterols in the plasma membrane make the membrane more firm
and prevent the membrane from freezing at low temperatures.
Plasma membranes often contain specific proteins embedded
within the lipid bilayer.
These proteins are called integral proteins.
Some integral proteins, such as cell surface markers, emerge
from only one side of the membrane.
Others, such as receptor proteins and transport proteins, extend
across the plasma membrane and are exposed to both the cell’s
interior and exterior environments.
Transmembrane proteins are integral proteins that cross the
membrane and can act as pathways for ions and molecules.
Polytopic (It is generally accepted that 'polytopic'
membrane proteins – the polypeptide chains of which cross
the membrane multiple times) transmembrane proteins cross
the membrane several times.
Some are receptor proteins while others form channels.
(A transmembrane protein (TP) is a type of integral
membrane protein that spans the entirety of the cell membrane ).
Proteins that extend across the plasma
membrane are able to detect
environmental signals and transmit
them to the inside of the cell.
Peripheral proteins, such as the
enzyme shown in Figure 4-11, lie on
only one side of the membrane and
are not embedded in it. As Figure 4-11
shows, integral proteins exposed to the
cell’s external environment often have
carbohydrates attached. These
carbohydrates can act as labels on cell
surfaces.
Some labels help cells recognize each
other and stick together.
Viruses can use these labels as docks
for entering and infecting cells.
Integral proteins play important roles Cell membranes often contain proteins. Integral proteins include cell-surface
in actively transporting markers, receptor proteins, and transport proteins. Enzymes are examples of
molecules into the cell. peripheral proteins.
Some act as channels or pores that allow certain substances to pass.
Other integral proteins bind to a molecule on the outside of the cell
and then transport it through the membrane.
Still others act as sites where chemical messengers such as
hormones can attach.
Many enzymes are proteins.
Enzyme reactions depend on a physical fit between the enzyme
molecule and its specific substrate, the reactant being catalyzed.
Notice that the enzyme has folds, or an active site, with a shape
that allows the substrate to fit into the active site.
An enzyme acts only on a specific substrate because only that
substrate fits into its active site.
The linkage of the enzyme and substrate causes a slight change
in the enzyme’s shape.
The change in the enzyme’s shape weakens some chemical
bonds in the substrate, which is one way that enzymes reduce
activation energy, the energy needed to start the reaction.
After the reaction, the enzyme releases the products.
An enzyme may not work if its environment is changed.
For example, change in temperature or pH can cause a change in
the shape of the enzyme or the substrate.
If such a change happens, the reaction that the enzyme would
have catalyzed cannot occur.
Different enzymes that catalyze the same chemical reaction are
called isozymes.
Integral membrane proteins that cross lipid bilayers feature
prominently in all aspects of cell biology.
Some are enzymes that synthesize lipids for biological
membranes.
Others serve as adhesion proteins that allow cells to interact
with each other or extracellular substrates.
Because cells need to sense hormones and many other
molecules that cannot penetrate a lipid bilayer, they have
evolved thousands of protein receptors that span the bilayer.
 Integral membrane proteins cross the lipid bilayer, and
peripheral membrane proteins associate with the inside or
outside surfaces of the bilayer.
 Transmembrane segments of integral membrane proteins
interact with hydrocarbon chains of the lipid bilayer and have
few hydrophilic residues on these surfaces.
Hormones or other extracellular signaling molecules
bind selectively to receptors exposed on the cell surface.
The energy from binding is used to transmit a signal
across the membrane and regulate biochemical reactions
in the cytoplasm.
Three families of pumps that use adenosine triphosphate
(ATP) hydrolysis as the source of energy to transport ions or
solutes up concentration gradients across membranes.

For example, pumps in the plasma membranes of animal cells

use ATP hydrolysis to expel Na+ and concentrate K+ in the
cytoplasm.
Another type of pump creates the acidic environment inside
lysosomes.
A related pump in mitochondria runs in the opposite direction,
taking advantage of a proton gradient across the membrane to
synthesize ATP.
A third family, called ABC transporters, use ATP hydrolysis to
move a wide variety of solutes across plasma membranes.
The ABC transporters are a class of active transporters that are
used by both prokaryotes and eukaryotes.
While prokaryotes use these transporters to import hydrophilic
molecules, both prokaryotes and eukaryotes use them to export
molecules such as lipids, steroids, and toxins.
A proton pump is an integral membrane protein pump that builds
up a proton gradient across a biological membrane.
ABC transporters are defined by the presence of nucleotide-
binding domains containing two conserved peptide motifs
known as Walker A and Walker B that are present in many
proteins that utilize ATP.
ABC transporters form a large and ubiquitous superfamily of
transporters that participate in a wide range of physiological
processes. Mammalian ABC transporters are involved in the
cellular export of several groups of molecules, including
cholesterol and sterols, lipids.
Carrier proteins facilitate the movement of ions and nutrients
across membranes, allowing them to move down
concentration gradients much faster than they can penetrate
the lipid bilayer.
Some carriers couple movement of an ion such as Na+ down its
concentration gradient to the movement of a solute such as
glucose up a concentration gradient into the cell.

Carriers change their shape reversibly, opening and closing

“gates” to transport their cargo across the membrane one
molecule at a time.
Channels are transmembrane proteins with selective
pores that allow ions, water, glycerol, or ammonia to move
very rapidly down concentration gradients across membranes.
Taking advantage of ion gradients created by pumps and
carriers, cells selectively open ion channels to create electrical
potentials across the plasma membrane and some organelle
membranes.
All living organisms depend on combinations of pumps, carriers,
and channels for many physiological functions.
Cells use ion concentration gradients produced by pumps as a
source of potential energy to drive the uptake of nutrients
through plasma membrane carriers.
Epithelial cells lining our intestines combine different carriers and
channels in their plasma membranes to transport sugars, amino
acids, and other nutrients from the lumen of the gut into the
blood.
Nerve and muscle cells create fast moving fluctuations in the
plasma membrane potential for high-speed communication;
operating on a millisecond time scale, voltage-gated ion
channels produce waves of membrane depolarization and
repolarization called action potentials.
Each of our physiological systems depends on this cooperation
among pumps, carriers and channels.
Membranes also partition the cytoplasm of eukaryotes into
compartments, including the nucleus and membrane
bounded organelles.
Each type of membrane is specialized for its various
functions, but all biological membranes have much in
common: a planar fluid bilayer of lipid molecules, integral
membrane proteins that cross the lipid bilayer, and
peripheral membrane proteins on both surfaces.
FIGURE 13.1 DEVELOPMENT OF
CONCEPTS IN MEMBRANE
STRUCTURE.
A, Gorder and Grendel model from
1926.
B, Davson and Danielli model from
1943 reflecting beliefs of the time
about the small sizes of proteins.
C, Singer and Nicholson fluid
mosaic model from 1972.
D, Contemporary model with
peripheral and integral membrane
proteins.
The lipid bilayer shown here and
used throughout the book is based
on a dynamic computational model
(Fig. 13.5). The density of proteins in
actual membranes is higher than
shown here.
Lipids form the framework of biological membranes, anchor
soluble proteins to the surfaces of membranes, store energy,
and carry information as extracellular hormones and as
intracellular second messengers.
Lipids are organic molecules generally are much more soluble in
organic solvents than in water.
They consist predominantly of aliphatic or aromatic
hydrocarbons.
The Plasma Membrane Is Reinforced by the Underlying
Cell Cortex

A cell membrane by itself is extremely thin and fragile.

It would require nearly 10,000 cell membranes laid on top of one
another to achieve the thickness of this paper.
Most cell membranes are therefore strengthened and supported by
a framework of proteins, attached to the membrane via
transmembrane proteins.
For plants, yeasts, and bacteria, the cell’s shape and mechanical
properties are conferred by a rigid cell wall—a fibrous layer of
proteins, sugars, and other macromolecules that encases the
plasma membrane.
By contrast, the plasma membrane of animal cells is stabilized by a
meshwork of filamentous proteins, called the cell cortex, that is
attached to the underside of the membrane.
The cortex of the human red blood cell has a relatively simple and
regular structure and has been especially well studied. Red blood
cells are small and have a distinctive flattened shape (Figure
11−29A).
The main component of their cortex is the dimeric protein spectrin,
a long, thin, flexible rod about 100 nm in length.
Spectrin forms a lattice that provides support for the plasma
membrane and maintains the cell’s biconcave shape.
The spectrin network is connected to the membrane through
intracellular attachment proteins that link spectrin to specific
transmembrane proteins.
The importance of this meshwork is seen in mice and humans that,
due to genetic alterations, produce a form of spectrin with an
abnormal structure.
These individuals are anemic: they
have fewer red blood cells than
normal. The red cells they do have are
spherical instead of flattened and are
abnormally fragile. Proteins similar to
spectrin, and to its associated
attachment proteins, are present in
the cortex of most animal cells. But
the cortex in these cells is especially
rich in actin and the motor protein
myosin, and it is much more complex
than that of red blood cells.
Figure 11–29 A cortex made largely of spectrin gives human red blood cells their characteristic shape.
(A) Scanning electron micrograph showing human red blood cells, which have a flattened, biconcave shape. These cells
lack a nucleus and other intracellular organelles. (B) In the cortex of a red blood cell, spectrin dimers (red) are linked end-
to-end to form longer tetramers. The spectrin tetramers, together with a smaller number of actin molecules, are linked
together into a mesh. This network is attached to the plasma membrane by the binding of at least two types of attachment
proteins (shown here in yellow and blue) to two kinds of transmembrane proteins (shown here in green and brown). (A,
courtesy of Bernadette Chailley.)
But the cortex in these cells is especially
rich in actin and the motor protein
myosin, and it is much more complex
than that of red blood cells. Whereas
red blood cells need their cortex mainly
to provide mechanical strength as they
are pumped through blood vessels,
other cells also use their cortex to
selectively take up materials from their
environment, to change their shape, and
to move. In addition, cells also use their
cortex to restrain the diffusion of
proteins within the plasma membrane.
Figure 11–29 A cortex made largely of spectrin gives human red blood cells their characteristic shape.
(A) Scanning electron micrograph showing human red blood cells, which have a flattened, biconcave shape. These cells
lack a nucleus and other intracellular organelles. (B) In the cortex of a red blood cell, spectrin dimers (red) are linked end-
to-end to form longer tetramers. The spectrin tetramers, together with a smaller number of actin molecules, are linked
together into a mesh. This network is attached to the plasma membrane by the binding of at least two types of attachment
proteins (shown here in yellow and blue) to two kinds of transmembrane proteins (shown here in green and brown). (A,
courtesy of Bernadette Chailley.)
Copyright © 2019 by Bruce Alberts, Dennis Bray, Karen Hopkin,
Alexander Johnson, the Estate of Julian Lewis, David Morgan,
Martin Raff, Nicole Marie Odile Roberts, and Peter Walter

pp.365-387
Thank you for attention