Figure 2

Characterization of the lipids bound to PASb-3α.
(a) Two neutral lipids (yellow bands on the iodine vapor stained plate) and two phosphorous-containing lipids (blue bands over white background) were carried over by the purified protein samples. The two phospholipids were identified as 18:1-lysophospholipds. (b) Free oleic and linoleic acids bind with low-nanomolar affinity to delipidated PASb-3α, suggesting that unsaturation is a mandatory feature for the partner fatty acid and, as unsaturation accumulates, the higher the affinity for the protein. (c) Boltzmann distributions representing the canonical ensembles of fatty acid desolvation. The estimated entropies decrease as the degree of unsaturation increase. Crossed-circles over the curves point out the frequency of putative bound-state enthalpy into the distribution.