Kinetics of the interaction of myelin basic protein with phospholipid layers

被引：3

作者：

Facci, P ^{[1
]}

Cavatorta, P

Cristofolini, L

Fontana, MP

Riccio, P

机构：

[1] Univ Parma, Dept Phys, I-43100 Parma, Italy

[2] Univ Parma, INFM, I-43100 Parma, Italy

[3] Univ Basilicata, Dept Biol, I-85100 Potenza, Italy

来源：

CHEMICAL PHYSICS LETTERS | 1999年 / 304卷 / 3-4期

关键词：

D O I：

10.1016/S0009-2614(99)00290-0

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The time dependence of the adsorption of myelin basic protein onto dipalmitoyl phosphatidyl glycerol multilayers has been followed directly, using a novel application of a microgravimetric gauge. Our results, supplemented by other data obtained by FTIR, show the ease and versatility of the quartz microbalance for investigating the interaction processes between proteins and phospholipid layers and show that the protein adsorption is accompanied by structural changes in the proteolipid ensemble and adsorbed liquid water; it is furthermore dependent on the mesoscopic defect morphology of the ensemble. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：197 / 201

页数：5

共 9 条

[1] FORMATION OF GLASSES FROM LIQUIDS AND BIOPOLYMERS [J].