BIOC 212 Lecture Notes - Lecture 24: Glycolipid, Phospholipid, Glycosylphosphatidylinositol

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14 Oct 2015
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< protein polarity (head groups) very polar, charged. +1 -1 or +1 -2 hydrophobicity very hydrophobic. < phospholipid varies greatly varies greatly phospholipids glycolipids cholesterol free fatty acids amino acid side chains. Membrane proteins: the sequence of a protein determines its structure, function and localization. Also for membrane proteins: structure of membrane proteins involves added contacts with lipids, localization of membrane proteins requires protein-based targeting mechanisms, terminology: soluble proteins are not associated with membranes mitochondrion and cytosol. Integral membrane proteins are tightly anchored by hydrophobic interactions with the interior of the lipid bilayer: 1 or more transmembrane -helices, transmembrane -barrel, amphipathic -helix in one face of the membrane. Hydrophobic on one side, polar on the other. Lipid-anchored: proteins are covalently linked to one or more lipids or fatty acid groups. Strength of anchor depends on number and type of lipid. With integral membrane proteins, can be strong interactions. With lipid head groups, weak interactions peripheral lipid-binding.

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