Fig. 2: CD spectra and MD simulated averaged structures of the first six patterns (x = 2–7). | Nature Communications

Fig. 2: CD spectra and MD simulated averaged structures of the first six patterns (x = 2–7).

From: Exo-chirality of the α-helix

Fig. 2

For all sequences (M-helices: A 7KNBD, B 3KNBD, and C 6KNBD top row; P-helices: D 5KNBD, E 4KNBD, and F 2KNBD bottom row): CD and UV–Vis spectra (top box). Zenithal and lateral views of the superposition of the structures in the trajectory of the MD simulation (one structure every 500 ns, backbone is represented as a gray cartoon and KNBD residues in color shades (bottom-left box). Zenithal and lateral views of the MD simulation averaged structure and the NBD centers of mass together with the exo-helical representation (bottom-right box). Structural parameters of the exo-helix (χ, r, P, and d) from the averaged structure are denoted. The calculated rotational angle of the oligo(glutamic acid) backbone (Ω) was close to the ideal value (99°), confirming the correct folding of the calculated α-helix core for all cases. θBB and θNBD expressed in deg × cm2 × dmol−1. εBB and εNBD expressed in cm2 × dmol−1.

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