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CHAPTER 5 THE DYNAMIC CELL MEMBRANE

Outside of cell

Carbohydrates are attached to the outer surface of proteins (forming glycoproteins) or lipids (forming glycolipids).

In animal cells, some membrane proteins associate with filaments in the extracellular matrix.

Some proteins adhere one cell to another.

Phospholipid bilayer

Inside of cell

Peripheral proteins do not penetrate the bilayer at all.

Cholesterol molecules interspersed among phospholipid tails in the bilayer influence the fluidity of fatty acids in the membrane.

Some membrane proteins interact with the interior cytoskeleton.

Some integral proteins cross the entire phospholipid bilayer; others penetrate only partially into the bilayer.

5.1 The Fluid Mosaic Model The general molecular structure of biological membranes is a continuous phospholipid bilayer in which proteins are embedded. (The purple ribbons represent structural elements of the cell and extracellular matrix.)

I Up to 25 percent of the lipid content of a membrane may be

cholesterol. When present, cholesterol is important to membrane integrity, and most cholesterol in membranes is not hazardous to your health. A molecule of cholesterol is commonly situated next to an unsaturated fatty acid (see Figure 5.1).

Because of these properties, one way in which phospholipids can coexist with water is to form a bilayer, with the fatty acid tails of the two layers interacting with each other and the polar heads facing the outside aqueous environment (Figure 5.2). In the laboratory, it is easy to make artificial bilayers with the same organization as natural membranes. In addition, small holes in a phospholipid bilayer seal themselves spontaneously. This capacity of lipids to associate with one another and maintain a bilayer organization helps biological membranes fuse during vesicle formation, phagocytosis, and related processes. All biological membranes have a similar structure, but membranes from different cells or organelles may differ greatly in their lipid composition:
I Phospholipids can differ in terms of fatty acid chain length,

You can rinse mud off your hands with plain water, but you cant get rid of grease that way because grease isnt watersoluble. Soap molecules have one end that is water-soluble and one end that is fat-soluble, making it possible to wash grease off with soap and water.

degree of unsaturation (double bonds) in the fatty acids, and the polar (phosphate-containing) groups present.

The phospholipid bilayer stabilizes the entire membrane structure, but leaves it flexible, not rigid. At the same time, the fatty acids of the phospholipids make the hydrophobic interior of the membrane somewhat fluidabout as fluid as lightweight machine oil. This fluidity permits some molecules to move laterally (side to side) within the plane of the membrane. A given phospholipid molecule in the plasma membrane can travel from one end of the cell to the

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Copyright 2008 Sinauer Associates Inc.

5.1 WHAT IS THE STRUCTURE OF A BIOLOGICAL MEMBRANE?

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5.2 A Phospholipid Bilayer Separates Two Aqueous Regions The eight phospholipid molecules shown here represent a small cross section of a membrane bilayer.

Aqueous environment

other in a little more than a second! On the other hand, seldom does a phospholipid molecule in one half of the bilayer flip over to the other side and trade places with another phospholipid molecule. For such a swap to happen, the polar part of each molecule would have to move through the hydrophobic interior of the membrane. Since phospholipid flip-flops are rare, the inner and outer halves of the bilayer may be quite different in the kinds of phospholipids they contain. The fluidity of a membrane is affected by its lipid composition and by its temperature. In general, shorter-chain fatty acids, unsaturated fatty acids, and less cholesterol result in more fluid membranes. Adequate membrane fluidity is essential for many membrane functions. Because molecules move more slowly and fluidity decreases at reduced temperatures, membrane functions may decline in organisms that cannot keep their bodies warm.To address this problem, some organisms simply change the lipid composition of their membranes under cold conditions, replacing saturated with unsaturated fatty acids and using fatty acids with shorter tails. Such changes play a part in the survival of plants and hibernating animals and bacteria during the winter.

The nonpolar, hydrophobic fatty acid tails interact with one another in the interior of the bilayer.

The charged, or polar, hydrophilic head portions interact with polar water.

Aqueous environment

Membrane proteins are asymmetrically distributed

All biological membranes contain proteins. Typically, plasma membranes have one protein molecule for every 25 phospholipid molecules. This ratio varies, however, depending on membrane function. In the inner membrane of the mitochondrion, which is specialized for energy processing, there is one protein for every 15 lipids. On the other hand, myelin, a membrane that encloses some neurons (nerve cells) and uses the properties of lipids to act as an electrical insulator, has only one protein per 70 lipids. Many membrane proteins are embedded in, or extend across, the phospholipid bilayer (see Figure 5.1). Like phospholipids, these proteins have both hydrophilic and hydrophobic regions.
I Hydrophilic regions: Stretches of amino acids with hydrophilic

bilayer of cellular membranes (Figure 5.3).The bumps that can be seen protruding from the interior of these membranes are not observed in pure lipid bilayers. According to the fluid mosaic model, the proteins and lipids in a membrane are independent of each other and interact only noncovalently. The polar ends of proteins can interact with the polar ends of lipids, and the nonpolar regions of both molecules can interact hydrophobically. There are two general types of membrane proteins:
I Integral membrane proteins have hydrophobic domains and

penetrate the phospholipid bilayer. Many of these proteins have long, hydrophobic -helical regions (see Section 3.2) that span the core of the bilayer. Their hydrophilic ends protrude into the aqueous environments on either side of the membrane (Figure 5.4).
I Peripheral membrane proteins lack hydrophobic domains and

side chains (see Table 3.2) give certain regions of the protein a polar character. Those regions, or domains, interact with water, sticking out into the aqueous extracellular environment or cytoplasm.
I Hydrophobic regions: Stretches of amino acids with hydropho-

are not embedded in the bilayer. Instead, they have polar or charged regions that interact with similar regions on exposed parts of integral membrane proteins or with the polar heads of phospholipid molecules (see Figure 5.1). Some membrane proteins are covalently attached to fatty acids or other lipid groups. These proteins can be classified as a special type of integral protein, as their hydrophobic lipid component allows them to insert themselves into the phospholipid bilayer. Proteins are asymmetrically distributed on the inner and outer surfaces of a membrane. Integral membrane proteins that protrude on both sides of the membrane, known as transmembrane proteins, show different faces on the two membrane surfaces. Such proteins have certain specific domains on the outer side of the mem-

bic side chains give other regions of the protein a nonpolar character. These domains interact with the fatty acid chains in the interior of the phospholipid bilayer, away from water. A special preparation method for electron microscopy, called
freeze-fracturing, reveals proteins embedded in the phospholipid

This material cannot be copied, disseminated, or used in any way without the express written permission of the publisher.

Copyright 2008 Sinauer Associates Inc.