Pressl K, Jørgensen K, Laggner P
Institute of Biophysics and X-ray Structure Research, Austrian Academy of Sciences, Graz.
Biochim Biophys Acta. 1997 Apr 3;1325(1):1-7. doi: 10.1016/s0005-2736(97)00013-8.
Simultaneous small- and wide-angle X-ray diffraction was used to investigate the structural conversions in the so-called sub-main-transition of fully hydrated multilamellar vesicles of distearoyl phosphatidylcholine (DSPC). The small-angle diffraction patterns show a modification in the supramolecular structure of the corrugated lipid bilayer and reveal that the sub-main-transition does not abolish the general features of the ripple phase (P(beta')). Concomitantly in the wide-angle region the diffraction patterns exhibit a rearrangement of the hydrocarbon chain packing and an onset of chain melting. The presence of KCl show an enhancement of the effects of the sub-main-transition. Moreover, in the ripple phase (P(beta')) below the sub-main-transition the hydrocarbon chains are positioned on an orthorhombic lattice in the presence of KCl.