Fig. 3: Computational evidence for the engagement of Gly22 and Phe20 of the E22G-Aβ40 in an NH-π interaction.
From: Direct detection of an NH-π hydrogen bond in an intrinsically disordered peptide
a Molecular Dynamics (MD) simulation frames showcasing NH-π interactions observed in three independent MD runs of the E22G peptide (see Supplementary Fig. 12 for the WT peptide). The color scheme represents interaction types and their respective geometric cutoff values for distance dCN and angle θ. b The model chosen for density functional theory (DFT)-based calculations satisfies the stringent cutoffs of dCN, θ and ϕ (dCN <4.3 Å, −25° <θ <25°, and ϕ > 120°). c Non-Covalent Interactions (NCI) analysis of the computed electron density distribution (ρ) for the truncated FAG peptide. Left, the reduced density gradient (RDG, s) versus \({{\rm{sign}}}({\lambda }_{2})\rho\) (see the text for definition; color scheme: blue, strong attractive interactions; green, weak interactions; red, strong repulsive interactions). Right, the RDG isosurface at s = 0.3 a.u.
