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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 5. — ProXp-ala binding to tRNA^Pro is sensitive to changes in A76. (A) Left: schematic of RNA duplex variants used in EMSA assays where one strand is fluorescently labeled at the 3′ end. Right: Results of EMSA binding assays plotting fraction of bound RNA as a function of ProXp-ala concentration; A76 (WT, green), ΔA76 (blue) and 3′pΔA76 (orange). Lines are Hill equation fits to the data; error bars are standard deviation of three replicates. (B) Overlaid ¹H-¹⁵N HSQC spectra for the amide nitrogens of Glu30 (top) and Lys71 (bottom) illustrate decreased CSPs upon A76 mutations: Free [U-¹⁵N]-ProXp-ala (black), [U-¹⁵N]-ProXp-ala in the presence of the ΔA76-microhelix^Pro (blue), 3′pΔA76-microhelix^Pro (orange), or WT (A76) microhelix^Pro (green). The arrows indicate the CSPs observed upon WT microhelix^Pro binding to free ProXp-ala.