Myelin basic protein reduces molecular motions in DMPA, an elastic neutron scattering study

We have studied the effect of physiological amounts of myelin basic protein (MBP) on pure dimyristoyl l-aphosphatidic acid (DMPA) vesicles using the elastic neutron scattering technique. Elastic scans have been performed in a wide temperature range (20-300 K). In the lower temperature region the behaviour of the integrated elastic intensity was the typical one of harmonic systems. The analysis of the Q and T dependence performed in terms of an asymmetric double well potential clearly showed that the effect of the protein consisted in a significant reduction of the conformational mobility of the DMPAbilayers and in the stabilisation of the membrane.