Editing Peripheral membrane protein (section)

===Covalently bound lipid anchors===
[[Lipid anchored protein]]s are covalently attached to different [[fatty acid]] [[acyl]] chains on the [[cytoplasm]]ic side of the [[cell membrane]] via [[palmitoylation]], [[myristoylation]], or [[prenylation]]. On the exoplasmic face of the cell membrane, lipid anchored proteins are covalently attached to the [[lipids]] [[glycosylphosphatidylinositol]] (GPI) and [[cholesterol]].<ref name="Silvius">{{cite book| vauthors = Silvius JR |chapter=Lipidated peptides as tools for understanding the membrane interactions of lipid-modified proteins |title=Current Topics in Membranes |volume=52 |pages=371–395 |publisher=Academic Press |year=2003 |isbn=978-0-12-643871-0}}</ref><ref name="Baumann">{{cite book| vauthors = Baumann NA, Mennon AK |chapter=Lipid modifications of proteins | veditors = Vance DE, Vance JE |title=Biochemistry of Lipids, Lipoproteins and Membranes |pages=37–54 |edition=4th |publisher=Elsevier Science |year=2002 |isbn=978-0-444-51139-3}}</ref> Protein association with membranes through the use of [[acyl]]ated residues is a [[reversible process (thermodynamics)|reversible process]], as the acyl chain can be buried in a protein's hydrophobic binding pocket after dissociation from the membrane. This process occurs within the beta-subunits of [[G-protein]]s<!-- ref -->. Perhaps because of this additional need for structural flexibility, lipid anchors are usually bound to the highly flexible segments of proteins tertiary structure that are not well resolved by [[protein crystallography|protein crystallographic studies]].