Characterization of a surfactant-protein complex by small-angle neutron scattering

被引：2
|
作者：
Watanabe, Y [1 ]
Otomo, T
Shimizu, S
Adachi, T
Sano, Y
Furusaka, M
机构：
[1] Natl Food Res Inst, Tsukuba, Ibaraki 3058642, Japan
[2] High Energy Accelerator Res Org, Neutron Sci Lab, Tsukuba, Ibaraki 3050801, Japan
[3] Nihon Univ, Coll Sci & Technol, Tokyo 1018306, Japan
来源：
JOURNAL OF PHYSICS AND CHEMISTRY OF SOLIDS | 1999年 / 60卷 / 8-9期
关键词：
protein; neutron scattering;
D O I：
10.1016/S0022-3697(99)00124-9
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
The interior structure of the complex of reduced carboxymethylated lysozyme with dodecyl sulfate was studied by small-angle neutron scattering. The scattering curve of dodecyl sulfate in the complex was similar to that of the micelle formed by pure dodecyl sulfate. The scattering of the protein in the complex was obtained in the D2O buffer solution that matches approximately the scattering length density of perdeuterated dodecyl sulfate. The Kratky plot revealed that the protein poly peptide in the complex is a wormlike chain with a persistence length of 1.6 nm. (C) 1999 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码：1383 / 1386
页数：4
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