期刊
PROTEIN SCIENCE
卷 13, 期 12, 页码 3314-3321出版社
WILEY
DOI: 10.1110/ps.041024904
关键词
protein structure/folding; prions; aggregation; amyloid; conformational disease; infrared spectroscopy
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.
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