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FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils
Author(s) -
Zandomeneghi Giorgia,
Krebs Mark R.H.,
McCammon Margaret G.,
Fändrich Marcus
Publication year - 2004
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.041024904
Subject(s) - beta sheet , fibril , dihedral angle , ramachandran plot , transthyretin , chemistry , amyloid (mycology) , protein structure , biophysics , crystallography , protein secondary structure , amyloid fibril , biochemistry , hydrogen bond , biology , molecule , amyloid β , medicine , inorganic chemistry , disease , organic chemistry , pathology , endocrinology
The presence of β‐sheets in the core of amyloid fibrils raised questions as to whether or not β‐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 β‐sheets in native proteins. This difference is evident from the amide I region of the infrared spectrum and relates to the distribution of the ϕ/ψ dihedral angles within the Ramachandran plot, the average number of strands per sheet, and possibly, the β‐sheet twist. These data imply that amyloid fibril formation from native β‐sheet proteins can involve a substantial structural reorganization.