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Cell Biology
Biological membranes
Lecture 9
14/3/2021
Chapter 7
Lecture 8 Biological Membranes
Surface view of
monolayers.
This sketch of a freeze-
fractured membrane
shows electron
micrographs of the E and
P faces from the plasma
membrane of a mouse
kidney tubule cell.
Individual proteins
imbedded in either face
show up as small
particles (TEMs).
Freeze-Fracture Analysis of a
Membrane.
Lecture 8 Biological Membranes
Figure 7-17 Freeze-fracture electron micrograph
of human red blood cells.
Note that the density of intramembrane particles
on the cytosolic (P) face is higher than on the
external (E) face.
Lecture 8 Biological Membranes
Fluid mosaic model of membranes
Three classes of membrane proteins:
Protein class Location Interactions
Integral
proteins (Y)
Embedded
within lipid
bilayer
Held in place by
the
hydrophobic
interactions
Peripheral
Proteins
(Z)
Located on
surface of
membrane
Linked
noncovalently
to the polar
groups of
phospholipids
and proteins
Lipid anchored
Proteins
(X)
On the
periphery but
anchored in the
lipid layer
hydrophilic
11_21_proteins.associ.jpg
Lecture 8 Biological Membranes
Membrane proteins can associate with the lipid bilayer in
several different ways
(A) Transmembrane proteins can extend across the bilayer as a single a helix,
as multiple a helices, or as a rolled-up b sheet (called a b barrel).
(B) Some membrane proteins are anchored to the cytosolic surface by an
amphipathic a helix.
(C) Others are attached to either side of the bilayer solely by a covalent
attachment to a lipid molecule (red zigzag lines).
(D) Finally, many proteins are attached to the membrane only by relatively
Figure 7-19 The Main Classes of Membrane Proteins
Membrane proteins are classified according to their mode of attachment to the membrane. Integral
membrane proteins contain one or more hydrophobic regions that are embedded within the lipid
bilayer. Peripheral membrane proteins are too hydrophilic to penetrate into the membrane but are
attached to the membrane by electrostatic and hydrogen bonds that link them to adjacent
membrane proteins or to phospholipid head groups. Lipid-anchored proteins are hydrophilic and do
not penetrate into the membrane; they are covalently bound to lipid molecules that are embedded
in the lipid bilayer. (f) Proteins on the inner surface of the membrane are usually anchored by either a
fatty acid or a prenyl group. (g) On the outer membrane surface, the most common lipid anchor is
glycosylphosphatidylinositol (GPI).
Lecture 8 Biological Membranes
Transmembrane protein
Lecture 8 Biological Membranes
 Hydrophobic amino acid
residues span membrane
 Hydrophilic domains on both
sides of membrane
 Only outer domain has
covalently attached carbohydrates
Extracted with detergents
Glycophorine one transmembrane span
a-helix
transmembrane
domain
Transmembrane proteins span the
bilayer
Lecture 8 Biological Membranes
Hydrophobic R
groups of amino
acid interact with
fatty acid chains
Integral membrane protein
Lecture 8 Biological Membranes
 Most membrane proteins have multiple
transmembrane spans.
More difficult to work with than water soluble
protein
Bacteriorodpsin
Peripheral protein
Lecture 8 Biological Membranes
 No transmembrane spans.
 Located on surface of membrane .
 Usually bound electrostatically to membrane.
Peripheral protein
Lecture 8 Biological Membranes
 No hydrophobic interactions with interior of
membrane
 bind to other proteins
 bind to lipid head groups.
 Peripheral proteins much easier to isolate (like
water soluble protein)
Lipid anchored proteins
Lecture 8 Biological Membranes
 Hydrophilic proteins that don’t penetrate into the
membranes.
 Covalently bound to lipid molecules that are
embedded in lipid bilayer.
Lecture 10, membranes
Functions of membrane proteins
13
Functions of membrane proteins
Lecture 10, membranes
Functions of membrane proteins
Lecture 10, membranes
Figure 11–20 Plasma membrane
proteins have a variety of
functions.
Lecture 10, membranes
Light transduction
Lecture 10, membranes
Absorb light:
 Rhodopsin: absorbed light triggers nervous
impulse.
 Bacteriorhodopsin: uses light energy to
transport H+ across membrane.
 Light harvesting proteins
 Reaction center proteins
Transfer light
energy to other
protein
Electron transport proteins
Lecture 10, membranes
Transfer e- from one molecule to another
molecule
examples:
 Cytochrome C
 Ferredoxin
 Plastocyanin
Receptor proteins
Lecture 10, membranes
 Bind other molecules
 Elicit cell response
example: acetylcholine receptor : opens
Na+ channels
Membrane carbohydrates
Lecture 10, membranes
 Approximately 2-10 % of mass
 Confined mainly to the non-cytosolic surface:-
- On the extracellular surface of the cells
- Inward toward the lumen of the compartment
Membrane carbohydrates
Lecture 10, membranes
 Covalent
linkage to
proteins and
lipids
Glycoproteins
Proteoglycans
Glycolipids
Externally bound
membrane carbohydrates
Lecture 10, membranes
Most carbohydrate
attached to protein
 Some
carbohydrates
attached to lipid
Glycophorin
In many animal cells, the carbohydrate groups of
plasma membrane glycoproteins and glycolipids
protrude from the cell surface and form a surface coat
called the glycocalyx (meaning “sugar coat”).
they are important components of the recognition
sites of membrane receptors, in antibody-antigen
reactions, and in intercellular adhesion to form tissues.
Glycocalyx surrounding
animal egg cell
Glycocalyx
Lecture 10, membranes
Lecture 10, membranes
Glycocalyx of Streptococcus enables it to escape
detection & destruction by immune system
Lecture 10, membranes
Membrane carbohydrates bound to
the internal surface of lipid bilayer
Lecture 10, membranes
Covalently bound carbohydrates to the
internal surface of
 Golgi vesicles
 Secretion vesicles
 Lysosomes also have
RBC plasma membrane composition
(by weight)
Lecture 10, membranes
1. 52% protein
2. 40% lipid
3. 8% carbohydrate by weight
Note: Most of the membrane mass IS NOT due to
lipids!!!
An erythrocyte is a small, disk-shaped cell with a diameter of
about 7 μm. A mammalian erythrocyte contains no nucleus or
other organelles, which makes it easy to obtain very pure
plasma membrane preparations without contamination by
organelle membranes.
Peripheral membrane proteins
Lecture 10, membranes
(Spectrin and actin are peripheral proteins associated
with membrane, but not in bilayer)
Structural Features of the Erythrocyte
Plasma Membrane
Lecture 10, membranes
integral proteins
a.Glycophorin
b.Anion channel
peripheral
proteins
a)Spectrin
b)Ankyrin
c)Actin
d)Band 4.1
Lecture 10, membranes
FIGURE 7-28
demonstration of the
mobility of membrane
proteins by cell fusion.
The mobility of
membrane proteins
can be shown
experimentally by the
mixing of membrane
proteins that occurs
when cells from two
different species
(mouse and human)
are fused and the
membrane proteins
are labeled with
specific fluorescent
antibodies.
Blood group antigens are
glycosphingolipids
Lecture 10, membranes
Lecture 10, membranes
Critical thinking
The effects of temperature and lipid composition on
membrane fluidity are often studied by using artificial
membranes containing only one or a few kinds of
lipids and no proteins. Assume that you have made
the following artificial membranes:
 Membrane 1: Made entirely from
phosphatidylcholine with saturated 16-carbon fatty
acids.
 Membrane 2: Same as membrane 1, except that
each of the 16-carbon fatty acids has a single cis
double bond.
 Membrane 3: Same as membrane 1, except that
each of the saturated fatty acids has only 14
carbon atoms.
Lecture 10, membranes
 After determining the transition temperatures of
samples representing each of the membranes, you
discover that your lab partner failed to record which
membranes the samples correspond to. The three
values you determined are –36°C, 23°C, and 41°C.
Assign each of these transition temperatures to the
correct artificial membrane, and explain your
reasoning.

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Lecture 10 membranes.pptx

  • 1. Cell Biology Biological membranes Lecture 9 14/3/2021 Chapter 7 Lecture 8 Biological Membranes
  • 2. Surface view of monolayers. This sketch of a freeze- fractured membrane shows electron micrographs of the E and P faces from the plasma membrane of a mouse kidney tubule cell. Individual proteins imbedded in either face show up as small particles (TEMs). Freeze-Fracture Analysis of a Membrane. Lecture 8 Biological Membranes
  • 3. Figure 7-17 Freeze-fracture electron micrograph of human red blood cells. Note that the density of intramembrane particles on the cytosolic (P) face is higher than on the external (E) face.
  • 4. Lecture 8 Biological Membranes Fluid mosaic model of membranes Three classes of membrane proteins: Protein class Location Interactions Integral proteins (Y) Embedded within lipid bilayer Held in place by the hydrophobic interactions Peripheral Proteins (Z) Located on surface of membrane Linked noncovalently to the polar groups of phospholipids and proteins Lipid anchored Proteins (X) On the periphery but anchored in the lipid layer hydrophilic
  • 5. 11_21_proteins.associ.jpg Lecture 8 Biological Membranes Membrane proteins can associate with the lipid bilayer in several different ways (A) Transmembrane proteins can extend across the bilayer as a single a helix, as multiple a helices, or as a rolled-up b sheet (called a b barrel). (B) Some membrane proteins are anchored to the cytosolic surface by an amphipathic a helix. (C) Others are attached to either side of the bilayer solely by a covalent attachment to a lipid molecule (red zigzag lines). (D) Finally, many proteins are attached to the membrane only by relatively
  • 6. Figure 7-19 The Main Classes of Membrane Proteins Membrane proteins are classified according to their mode of attachment to the membrane. Integral membrane proteins contain one or more hydrophobic regions that are embedded within the lipid bilayer. Peripheral membrane proteins are too hydrophilic to penetrate into the membrane but are attached to the membrane by electrostatic and hydrogen bonds that link them to adjacent membrane proteins or to phospholipid head groups. Lipid-anchored proteins are hydrophilic and do not penetrate into the membrane; they are covalently bound to lipid molecules that are embedded in the lipid bilayer. (f) Proteins on the inner surface of the membrane are usually anchored by either a fatty acid or a prenyl group. (g) On the outer membrane surface, the most common lipid anchor is glycosylphosphatidylinositol (GPI). Lecture 8 Biological Membranes
  • 7. Transmembrane protein Lecture 8 Biological Membranes  Hydrophobic amino acid residues span membrane  Hydrophilic domains on both sides of membrane  Only outer domain has covalently attached carbohydrates Extracted with detergents Glycophorine one transmembrane span
  • 8. a-helix transmembrane domain Transmembrane proteins span the bilayer Lecture 8 Biological Membranes Hydrophobic R groups of amino acid interact with fatty acid chains
  • 9. Integral membrane protein Lecture 8 Biological Membranes  Most membrane proteins have multiple transmembrane spans. More difficult to work with than water soluble protein Bacteriorodpsin
  • 10. Peripheral protein Lecture 8 Biological Membranes  No transmembrane spans.  Located on surface of membrane .  Usually bound electrostatically to membrane.
  • 11. Peripheral protein Lecture 8 Biological Membranes  No hydrophobic interactions with interior of membrane  bind to other proteins  bind to lipid head groups.  Peripheral proteins much easier to isolate (like water soluble protein)
  • 12. Lipid anchored proteins Lecture 8 Biological Membranes  Hydrophilic proteins that don’t penetrate into the membranes.  Covalently bound to lipid molecules that are embedded in lipid bilayer.
  • 13. Lecture 10, membranes Functions of membrane proteins 13
  • 14. Functions of membrane proteins Lecture 10, membranes
  • 15. Functions of membrane proteins Lecture 10, membranes
  • 16. Figure 11–20 Plasma membrane proteins have a variety of functions. Lecture 10, membranes
  • 17. Light transduction Lecture 10, membranes Absorb light:  Rhodopsin: absorbed light triggers nervous impulse.  Bacteriorhodopsin: uses light energy to transport H+ across membrane.  Light harvesting proteins  Reaction center proteins Transfer light energy to other protein
  • 18. Electron transport proteins Lecture 10, membranes Transfer e- from one molecule to another molecule examples:  Cytochrome C  Ferredoxin  Plastocyanin
  • 19. Receptor proteins Lecture 10, membranes  Bind other molecules  Elicit cell response example: acetylcholine receptor : opens Na+ channels
  • 20. Membrane carbohydrates Lecture 10, membranes  Approximately 2-10 % of mass  Confined mainly to the non-cytosolic surface:- - On the extracellular surface of the cells - Inward toward the lumen of the compartment
  • 21. Membrane carbohydrates Lecture 10, membranes  Covalent linkage to proteins and lipids Glycoproteins Proteoglycans Glycolipids
  • 22. Externally bound membrane carbohydrates Lecture 10, membranes Most carbohydrate attached to protein  Some carbohydrates attached to lipid Glycophorin
  • 23. In many animal cells, the carbohydrate groups of plasma membrane glycoproteins and glycolipids protrude from the cell surface and form a surface coat called the glycocalyx (meaning “sugar coat”). they are important components of the recognition sites of membrane receptors, in antibody-antigen reactions, and in intercellular adhesion to form tissues. Glycocalyx surrounding animal egg cell
  • 26. Glycocalyx of Streptococcus enables it to escape detection & destruction by immune system Lecture 10, membranes
  • 27. Membrane carbohydrates bound to the internal surface of lipid bilayer Lecture 10, membranes Covalently bound carbohydrates to the internal surface of  Golgi vesicles  Secretion vesicles  Lysosomes also have
  • 28. RBC plasma membrane composition (by weight) Lecture 10, membranes 1. 52% protein 2. 40% lipid 3. 8% carbohydrate by weight Note: Most of the membrane mass IS NOT due to lipids!!! An erythrocyte is a small, disk-shaped cell with a diameter of about 7 μm. A mammalian erythrocyte contains no nucleus or other organelles, which makes it easy to obtain very pure plasma membrane preparations without contamination by organelle membranes.
  • 29. Peripheral membrane proteins Lecture 10, membranes (Spectrin and actin are peripheral proteins associated with membrane, but not in bilayer)
  • 30. Structural Features of the Erythrocyte Plasma Membrane Lecture 10, membranes integral proteins a.Glycophorin b.Anion channel peripheral proteins a)Spectrin b)Ankyrin c)Actin d)Band 4.1
  • 31. Lecture 10, membranes FIGURE 7-28 demonstration of the mobility of membrane proteins by cell fusion. The mobility of membrane proteins can be shown experimentally by the mixing of membrane proteins that occurs when cells from two different species (mouse and human) are fused and the membrane proteins are labeled with specific fluorescent antibodies.
  • 32. Blood group antigens are glycosphingolipids Lecture 10, membranes
  • 33. Lecture 10, membranes Critical thinking The effects of temperature and lipid composition on membrane fluidity are often studied by using artificial membranes containing only one or a few kinds of lipids and no proteins. Assume that you have made the following artificial membranes:  Membrane 1: Made entirely from phosphatidylcholine with saturated 16-carbon fatty acids.  Membrane 2: Same as membrane 1, except that each of the 16-carbon fatty acids has a single cis double bond.  Membrane 3: Same as membrane 1, except that each of the saturated fatty acids has only 14 carbon atoms.
  • 34. Lecture 10, membranes  After determining the transition temperatures of samples representing each of the membranes, you discover that your lab partner failed to record which membranes the samples correspond to. The three values you determined are –36°C, 23°C, and 41°C. Assign each of these transition temperatures to the correct artificial membrane, and explain your reasoning.