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. 2022 Nov 14;14(1):2143006. doi: 10.1080/19420862.2022.2143006

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© 2022 Genentech. Published with license by Taylor & Francis Group, LLC.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Conformational space that enables near-attack distances increasing the propensity for succinimide formation. a) The structural orientation of the reactive (1a and 2a) and non-reactive (2b and 3) side-chain conformations, characterized by ψ & χ, for an aspartic acid residue shown in ball and stick representation. b) Free-energy surface in the space of ψ & χ dihedral angles and c) the corresponding distance between Cγ and the n + 1 amide nitrogen calculated from metadynamics simulation of Ace-GGNAG-Nme pentapeptide.