Abstract
Dimyristoylphosphatidylcholine (DMPC) – polylysine and DMPC–histones systems have been studied by Raman spectroscopy and differential scanning calorimetry. The results of both techniques indicate that the interactions are mainly confined to the lipid–water interface. The protein fraction of histones giving rise to a partial penetration into the bilayer is not the lysine-rich fraction but rather the non-polar component of the proteins. On the basis of the results obtained, the formation of lipoprotein complexes between histones and DMPC appears to be ruled out.
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