Structure and Dynamics of Aβ(1-40) Oligomers Studied by Top-Down Hydrogen Exchange Mass Spectrometry

摘要

The DHX pattern is consistent with a β-turn-β motif for L 17 to M35. The N-terminus is involved in hydrogen bonding as well, whereas protection gradually tapers off for the C-terminal residues 35-40. Our data are consistent with earlier proposals, according to which Aβ(1-40) oligomers adopt a β-barrel structure. Overall, this study demonstrates how top-down MS with precursor ion selection can yield structural information for specific protein conformers in heterogeneous samples.