Essential Cell Biology 5th edition

376 CHAPTER 11 Membrane Structure
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.
• 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 proteins;
they can be released from the membrane by more gentle extraction
procedures that interfere with protein–protein interactions but leave the
lipid bilayer intact.
(A) (B) (C) (D)
MONOLAYER-
TRANSMEMBRANE
ASSOCIATED
LIPID-LINKED PROTEIN-ATTACHED
NH 2
EXTRACELLULAR SPACE
P
P
lipid
bilayer
CYTOSOL
COOH
integral membrane proteins
peripheral membrane proteins
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.