ANAT 212 Lecture Notes - Lecture 7: Integral Membrane Protein, Lipid Bilayer, Secretion
30 Mar 2020
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Document Summary
Transmembrane helix h-bonds that are holding the helix together (between every turn of the helix) the hydrophobic residues are all pointing out since the helix is inserted in the membrane. The hydrophobic amino acids are interacting with the inside of the lipid bilayer. So, when we remove that transmembrane helix out of the membrane all those hydrophobic amino acids are in contact with water so, they are not stable (hydrophobic amino acids need to be covered up ). Transmembrane barrel even though it is a different structure, there are also going to be hydrophobic residues exposed to water when we pull off the membrane. Membrane proteins are not stable when pulled out of the membrane (today lecture: how do we get a protein into the membrane) Lipid anchored proteins proteins with fatty acid chains or acyl chains attached to them.
