Structural, Dynamic Properties of Key Residues in Aβ Amyloidogenesis: Implications of an Important Role of Nanosecond Timescale Dynamics

Abstract

Flexibility exercise. NMR studies of the Aβ(1–40) and -(1–42) peptides demonstrated that structural, dynamic properties of soluble monomeric Aβ peptides are highly correlated to the amyloid fibril structure. In particular, fast-timescale dynamics were found to be an additional critical parameter in identifying the more crucial aggregation-prone segments of Aβ peptides (see figure). This method can be applied to investigate amyloidogenic and nonamyloidogenic properties of disordered states of proteins.