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.
Myelin basic protein reduces molecular motions in DMPA, an elastic neutron scattering study
2001
Abstract
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.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
