Structure of amyloid fibrils of hen egg white lysozyme studied by microbeam X-ray diffraction

被引：18

作者：

Yagi, Naoto ^{[1
]}

Ohta, Noboru ^{[1
]}

Matsuo, Tatsuhito ^{[1
]}

机构：

[1] SPring 8 JASRI, Res & Utilizat Div, Japan Synchrotron Radiat Res Inst, Sayo, Hyogo 6795198, Japan

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2009年 / 45卷 / 01期

关键词：

Spherulite; X-ray diffraction; beta-Sheet; CROSS-BETA CONFORMATION; PROTEIN SOLUTIONS; BOVINE INSULIN; CORE; SPHERULITES; FILAMENTS; FRAGMENT; DOMAIN; FIBER;

D O I：

10.1016/j.ijbiomac.2009.04.007

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Structure of spherical aggregates formed by hen egg white lysozyme(HEWL)was studied with microbeam X-ray diffraction. Aggregates with a diameter of 50-100 mu m were formed after incubation of HEWL at pH 1.6 and 60 degrees C up to 60 days. The scattering from the aggregate in solution showed a marked symmetry demonstrating it as a spherulite. A reflection at 1/0.46 nm(-1) along the fiber axis showed the presence of beta-sheets along the fiber. There were strong equatorial reflections at 1/2.4 and 1/1.2 nm(-1). The similarities to other amyloid fibers suggest that molecules are planar in the direction perpendicular to the fiber axis and beta-strands are making hydrogen bonds to neighboring molecules. (C) 2009 Elsevier B.V. All rights reserved.

引用

页码：86 / 90

页数：5

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