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. 2023 Mar 23;51(8):3988–3999. doi: 10.1093/nar/gkad192

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© The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research.

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

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Figure 6. — CSPs show parallel ProXp-ala-tRNA^Pro binding deficiencies upon deletion of A76 and mutation of K45. (A) Schematic of minihelix^Pro, which is indistinguishable from microhelix^Pro in terms of its binding to ProXp-ala (Supplementary Fig. 4). (B) Secondary structure of Cc ProXp-ala (top) and summary of per residue CSPs induced by minihelix^Pro binding to WT (green) and K45A (orange) ProXp-ala. (C) Spectral expansions of Gly84 (top), Lys71 (middle) and Leu47 (bottom) from overlaid ¹H–¹⁵N HSQC spectra of WT ProXp-ala (left and middle spectra) free (black), and in the presence of microhelix^Pro (green) or ΔA76-microhelix^Pro (blue), and of K45A ProXp-ala (right spectra) free (black), and in the presence of minihelix^Pro-bound (orange).