Complex systems lipid-protein mixtures and cell membranes

6 Complex systems lipid-protein mixtures and cell membranes 

These results have been extended and confirmed by numerous further studies. When intrinsic proteins interact with lipid mixtures that are partially immiscible, e.g. l-palmitoyl-2-oleoyl PC (POPC) and POPE, the calorimetric data suggest that the packing defects at domain boundaries could facilitate the direct interaction of the transmembrane regions of integral proteins with the lipid hydrophobic chains. Thus lipid domain formation would help in the membrane insertion of proteins. 

Ronald N. McElhaney and co-workers have refined the DSC studies of the effects of intrinsic proteins on the gel-fluid transition of phospholipids, using synthetic 

CH4 DIFFERENHAL SCANNING CALORIMETRY IN THE STUDY OF LIPID STRUCTURES 

Many other peptides whose mode of interaction with the lipid hilayer differs from that of the transmemhrane a-helices, e.g. cyclic antibiotic peptides, have also been stndied by DSC from the point of view of their interaction with saturated PC. Not unexpectedly, several different patterns of thermogram alteration have been obtained, witnessing the varying ways of interaction of those peptides with the phospholipid bilayer. 

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