Structure of amyloid fibrils

被引：0
|
作者：
Meinhardt, J. [2 ]
Faendrich, M. [1 ]
机构：
[1] Max Planck Forschungsstelley Enzymol Proteinfaltu, D-06120 Halle, Germany
[2] Fritz Lipmann Inst, Leibniz Inst Altersforsch, Jena, Germany
来源：
PATHOLOGE | 2009年 / 30卷 / 03期
关键词：
Alzheimer; Neurodegeneration; Prion; Protein folding; Aggregation; BETA; PROTEIN; PROTOFIBRILS; AGGREGATION; REVEALS;
D O I：
10.1007/s00292-009-1127-2
中图分类号：
R36 [病理学];
学科分类号：
100104 ;
摘要：
Amyloid fibrils are structurally defined as fibrillar polypeptide aggregates with a characteristic cross-beta structure. Such fibrils can be formed by certain polypeptide sequences in the human body and by numerous polypeptide sequences in vitro. All amyloid fibrils possess a structural spine that is formed by a cross-beta structure. This structure is stabilized by hydrogen bonds between the polypeptide backbone. In recent years, various biophysical techniques, such as X-ray crystallography, solid state nuclear magnetic resonance spectroscopy and electron cryo-microscopy have provided insights into the structural organization of amyloid fibrils. This review presents an overview of important results obtained with these methods.
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页码：175 / +
页数：6
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