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Chapter 10 Membrane Structure
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All biological membranes have a common structure – each is a very thin
film of lipid and protein molecules held together by noncovalent interactions
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Membrane lipids are amphipathic molecules, most of which
The Lipid Bilayer Membrane lipids are amphipathic molecules, most of which spontaneously form bilayers
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The most abundant membrane lipids are the phospholipids
Phospholipids have a polar head group and two hydrophobic hydrocarbon tails
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The tails are usually fatty acids, and
they can differ in length. One tail usually has one or more cis-double bonds, while the other does not.
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The shape and amphipathic nature of the
lipid molecules cause them to form bilayers spontaneouly in aqueous environments.
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Hydrophilic and hydrophobic molecules interact differently with water
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molecules spontaneously form bilayers in aqueous environments
Packing arrangements of lipid molecules in an aqueous environment Lipid molecules spontaneously aggregate to bury their hydrophobic tails in the interior and expose their hydrophilic heads to water. Being cylindrical, phospholipid molecules spontaneously form bilayers in aqueous environments
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the phospholipid molecule
The spontaneous closure of a phospholipid bilayer to form a sealed compartment The formation of a sealed compartment is fundamental to the creation of a living cell, and this behavior follows directly from the shape and amphipathic nature of the phospholipid molecule
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The lipid bilayer is a two-dimensional fluid
Individual lipid molecules are able to diffuse freely within lipid bilayers. Demonstrated using synthetic lipid bilayers and electron spin resonance (ESR) spectroscopy Liposomes
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A black membrane
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Phospholipid mobility
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The fluidity of a lipid bilayer depends on its composition and its temperature
The membrane becomes more difficult to freeze if the hydrocarbon chains are short or have double bonds, so that the membrane remains fluid at lower temperatures
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phospholipids, it often also contains cholesterol and glycolipids
The lipid bilayer of many cell membranes is not composed exclusively of phospholipids, it often also contains cholesterol and glycolipids
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Eucaryotic plasma membranes contain large amounts of cholesterol
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Four major phospholipids predominate in the plasma membrane of mammalian cells
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Lipid bilayers can form domains of different compositions
Lipid phase separation in artificial lipid bilayers (A) 1:1 mixture of phosphatidylcholine and sphingomyelin (B) 1:1:1 mixture of phosphatidylcholine, sphingomyelin, and cholesterol
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cholesterol, and some membrane proteins
Plasma membrane contains lipid rafts that are enriched in sphingolipids, cholesterol, and some membrane proteins Lipid rafts are small specialized areas in membranes where some lipids (primarily sphingolipids and cholesterol) and proteins are concentrated
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Lipid droplets are surrounded by a phospholipid monolayer
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The asymmetry of the lipid bilayer is functionally important
The lipid bilayer of human red blood cells
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Signaling functions of inositol phospholipids in the cytosolic leaflet of the plasma membrane
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Glycolipids are found on the surface of all plasma membranes
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Membrane Proteins
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Membrane proteins can be associated with the lipid bilayer in various ways
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Covalent attachment of a protein to the membrane by a
fatty acid chain or a prenyl group
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in an α-helical conformation
In most transmembrane proteins the polypeptide chain crosses the lipid bilayer in an α-helical conformation
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Membrane regions and preferred amino-acid locations
Membrane regions and preferred amino-acid locations. A snapshot of a lipid bilayer membrane and its three major regions. Grey, carbon atoms; red, oxygen; white, hydrogen bound to oxygen; orange, phosphorus. In an a-helix, 20 amino acids (blue) can span the hydrocarbon core, and 10 amino acids (green) can span the interfacial region. Arrows indicate where most of each amino acid (denoted by its three-letter symbol) would be found at equilibrium based on transfer free-energy measurements (Nature, 2005, Vol 433, )
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A possible scheme for the membrane-insertion decision, as proposed by Hessa et al. A top view of the membrane and the translocon pore that crosses it. Inside the pore is a peptide helix surrounded by water. The pore opens sideways into the membrane, allowing the helix to interact with the membrane lipids. If the peptide is more compatible with lipid than with water, it will transfer into the membrane; otherwise, it will continue to be moved through the pore. The figure is only intended to convey the basic principle, and omits many mechanistic and structural issues. (Nature, 2005, Vol 433, )
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Hydropathy plots identify potential α-helical segments in a polypeptide chain
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Two a helices in the aquaporin water channel, each of which spans only
halfway through the lipid bilayer
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Converting a single-chain multipass protein into a two-chain multipass protein
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Steps in the folding of a multipass transmembrane protein
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hydrogen-binding requirements is for multiple transmembrane strands
An alternative way for peptide bonds in the lipid bilayer to satisfy their hydrogen-binding requirements is for multiple transmembrane strands of polypeptide chains to be arranged as β sheet in the form of a closed barrel
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Many membrane proteins are glycosylated and have intrachain or interchain
disulfide bonds
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The cell coat, or glycocalyx is the carbohydrate-rich zone on the cell surface
Likely functions – protect cells against mechanical and chemical damage keep foreign objects and other cells at a distance
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A simplified diagram of the cell coat (glycocalyx)
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Membrane proteins can be solubilized and purified in detergents
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Structure and function of detergent micelles
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Solubilizing membrane proteins with a mild detergent
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functional membrane systems
The use of mild detergents for solubilizing, purifying, and reconstituting functional membrane systems
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that contain bacteriorhodopsin molecules
Bacteriorhodopsin is a proton pump that traverses the lipid bilayer as seven α helices The archaean Halobacterium salinarum showing patches of purple membrane that contain bacteriorhodopsin molecules
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The three-dimensional structure of a bacteriorhodopsin molecule
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Rhodopseudomonas viridis
Membrane proteins often function as large complexes The three-dimensional structure of the photosynthetic reaction center of the bacterium Rhodopseudomonas viridis
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Many membrane proteins diffuse in the plane of the membrane
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Fluorescence recovery after photobleaching
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Fluorescence loss in photobleaching
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Plasma membrane proteins are restricted to particular membrane
domains
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Three domains in the plasma membrane of a sperm cell
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Four ways of restricting the lateral mobility of specific plasma
membrane proteins
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The cytosolic side of plasma membrane proteins can be studied in red blood
cell ghosts
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The spectrin-based cytoskeleton on the cytosolic side of the human RBC membrane
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