Fatty acid-binding proteins protein folding

Li, H. L. and Frieden, C. (2007) Observation of sequential steps in the folding of intestinal fatty acid binding protein using a slow folding mutant and F-19 NMR. Proceedings of the National Academy of Sciences of the U. S. A., 104(29), 11993-11998. 

Palmitoylation is, after myristoylation, the most common modification of the a-sub-rmit of the heterotrimeric G-proteins (see chapter 5). The a-subunit of G-proteins can be lipidated in a two-fold marmer, with a myristoic acid and a pahnitoic acid anchor at the N-terminus. It appears in this case that two lipid anchors are necessary to mediate a stable association of the protein with the membrane. The lipidation of cytoplasmic protein tyrosine kinase also includes both myristoylation and palmitoylation. H-Ras protein also requires, apart from C-terminal farnesylation (see below), a pahnitoyl modification in order to bind to the plasma membrane. In all mentioned examples the fatty acid anchors play an essential role in the signal transduction. 

Computational and experimental studies of AEA and its parent fatty acid AA in a variety of environments indicate that these molecules are highly flexible and able to adopt both extended and folded shapes. Environment plays a strong role in the shape that AEA or AA takes, for, despite the fact that the shape of the binding cavity/crevice of the proteins with which AEA or AA complexes are quite different, these molecules can easily alter their conformation to adapt to each... 

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