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

被引：10

作者：

Natali, F

Gliozzi, A

Rolandi, R

Cavatorta, P

Deriu, A

Fasano, A

Riccio, P

机构：

[1] INFM, OGG, F-38042 Grenoble 9, France

[2] Univ Genoa, Dipartimento Fis, Genoa, Italy

[3] Univ Genoa, Unita INFM, Genoa, Italy

[4] Univ Parma, Dipartimento Fis, Parma, Italy

[5] Univ Parma, Unita INFM, Parma, Italy

[6] Dipartimento Biochim & Biol Mol, Bari, Italy

[7] Univ Basilicata, Dipartimento Biol Difesa Biotecnol Agroforetali, Potenza, Italy

来源：

PHYSICA B | 2001年 / 301卷 / 1-2期

关键词：

myelin; myelin basic protein; lipids; neutron scattering;

D O I：

10.1016/S0921-4526(01)00528-2

中图分类号：

O469 [凝聚态物理学];

学科分类号：

070205 ;

摘要：

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 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 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 Elsevier Science B.V. All rights reserved.

引用

页码：145 / 149

页数：5

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