FTIR reveals structural differences between native β-sheet proteins and amyloid fibrils

被引：586

作者：

Zandomeneghi, G

Krebs, MRH

Mccammon, MG

Fändrich, M

机构：

[1] IMB, D-07745 Jena, Germany

[2] Univ Cambridge, Cavendish Lab, P&C Grp, Cambridge CB3 0HE, England

[3] Univ Cambridge, Dept Chem, Cambridge CB2 1EW, England

来源：

PROTEIN SCIENCE | 2004年 / 13卷 / 12期

关键词：

protein structure/folding; prions; aggregation; amyloid; conformational disease; infrared spectroscopy;

D O I：

10.1110/ps.041024904

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：

The presence of beta-sheets in the core of amyloid fibrils raised questions as to whether or not beta-sheet-containing proteins, such as transthyretin, are predisposed to form such fibrils. However, we show here that the molecular structure of amyloid fibrils differs more generally from the beta-sheets in native proteins. This difference is evident from the amide I region of the infrared spectrum and relates to the distribution of the dihedral angles within the Ramachandran plot, the average number of strands per sheet, and possibly, the beta-sheet twist. These data imply that amyloid fibril formation from native beta-sheet proteins can involve a substantial structural reorganization.

引用

页码：3314 / 3321

页数：8

共 62 条

[1] Amyloidosis of Alzheimer's Aβ peptides:: solid-state nuclear magnetic resonance, electron paramagnetic resonance, transmission electron microscopy, scanning transmission electron microscopy and atomic force microscopy studies [J].