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. Author manuscript; available in PMC: 2011 Apr 15.
Published in final edited form as: Arch Biochem Biophys. 2010 Feb 11;496(2):84–92. doi: 10.1016/j.abb.2010.02.001

Table 1. Distribution of secondary structure elements in Aβ1-42 preparations as determined by the CD spectroscopy.

Peptide Aβ1-42 α-helix β-sheet Turn Unordered
Aβ1-42 monomers 71 % 13% 8% 8%
Aβ1-42 small oligomers,
protocol I 		4% 43% 21% 32%
Aβ1-42 larger oligomers,
protocol II 		4% 43% 21% 32%