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BCH2011: Textbook summary - Lecture 28

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LECTURE 28 Fluid Mosaic Lipid: Phospholipids form a bilayer in which the nonpolar regions of the lipid molecules in each layer face the core of the bilayer and their polar head groups face outward, interacting with the aqueous phase on either side. Proteins are embedded in this bilayer sheet, held by hydrophobic interactions between the membrane lipids and hydrophobic domains in the proteins. Some proteins protrude from only one side of the membrane; others have domains exposed on both sides. The orientation of proteins in the bilayer is asymmetric, giving the membrane ‘sideness’: the protein domains exposed on one side of the bilayer are different from those exposed on the other side, reflecting functional symmetry. The membrane mosaic is fluid because most of the interactions among its components are noncovalent, leaving individual lipid and protein molecules free to move laterally in the plane of the membrane. Integral Proteins: They are firmly associated with the lipid bilayer and are removable only by agents that interfere with hydrophobic interactions, such as detergents, organic solvents, or denaturants. Glycophorin: Its amino-terminal domain (bearing the carbohydrate chains) is on the outer surface and is cleaved by trypsin. The carboxyl terminus protrud
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