We have studied the effect of physiological amounts of myelin basic protein (MBP) on pure dimyristoyl L-α-phosphatidic 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 DMPA bilayers and in the stabilisation of the membrane. © 2001 Elsevier Science B.V.
CITATION STYLE
Natali, F., Gliozzi, A., Rolandi, R., Cavatorta, P., Deriu, A., Fasano, A., & Riccio, P. (2001). Myelin basic protein reduces molecular motions in DMPA, an elastic neutron scattering study. In Physica B: Condensed Matter (Vol. 301, pp. 145–149). https://doi.org/10.1016/S0921-4526(01)00528-2
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