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Nanotechnology-Enabled Sensors

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7.4 Proteins in <strong>Nanotechnology</strong> <strong>Enabled</strong> <strong>Sensors</strong> 429<br />

Fig. 7.49 A cross section of a membrane showing the phospholipid bilayer.<br />

A group of the transmembrane proteins consist of polypeptide chains<br />

which cross the bilayer and usually have an α-helix form. In many transmembrane<br />

proteins the polypeptide chain crosses the membrane only once.<br />

This type of protein can be a receptor for the extracellular signals. Other<br />

trans-membrane proteins form pores that allow water-soluble molecules to<br />

cross the membrane. Such pores cannot be formed by proteins with a single,<br />

uniformly hydrophobic transmembrane α-helix. Instead, these proteins<br />

generally have α-helices that cross the bilayer a few times. Some of these<br />

α-helices have both hydrophobic and hydrophilic side chains. The hydrophobic<br />

chains are close to the bilayer lipids and hydrophilic chains are located<br />

inside the cell. These pores function as selective transporters of small<br />

water-soluble molecules across the membrane. The subunits made of such<br />

helices are denoted as β, γ, and so on.

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