BIOL-UA 22 Chapter Notes - Chapter 10: Protein Aggregation, Antibody, Phosphatidylinositol
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22 Mar 2016
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Proteins interact with membranes in three different ways. Integral membrane proteins span the phospholipid bilayer and are made of three segments (i) (ii) cytosolic and exoplasmic domains have hydrophilic exterior surfaces that interact with the aqueous environment on the two faces of the membranes. C-terminus of the helix these groups are shielded from the hydrophobic interior of the membrane proteins with alpha-helical domains: glycophorin a. Aquaporin 0 = most abundant protein in plasma membrane of fiber cells that make up the lens of the mammalian eyes: protein"s surface is not covered by a set of uniform binding sites for phospholipid molecules. Instead, fatty acyl side chains pack tightly against irregular hydrophobic outer surface of the protein; lipids are annular phospholipids because they form a tight ring (annulus) of lipids that exchange less easily with bulk phospholipid in the bilayer. Gpi anchors are necessary for sufficient for binding proteins to membranes. Lipid-binding motifs help target peripheral proteins to the membrane.