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

We have studied the effect of physiological amounts of myelin basic protein (MBP) on pure dimyristoyl L-alpha -phosphatidic acid (DMPA) vesicles using the elastic neutron scattering technique. Elastic scans have been performe d in a wide temperature range (20-300 K). In the lower temperature region t he behaviour of the integrated elastic intensity was the typical one of har monic systems. The analysis of the e 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 DMPA bilayers and in the stabilisation of the membrane. (C) 2001 El sevier Science B.V. All rights reserved.