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. 2020 Mar 14;48(8):4521–4537. doi: 10.1093/nar/gkaa155

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© The Author(s) 2020. 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 (http://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. — (A) Combined amide chemical shift difference between the WT PTB RRM1 protein and the P142G (green) and L151G (blue) mutant proteins both in their RNA free state. (B) Smoothed secondary ¹³C chemical shift values (Δ¹³Cα–Δ¹³Cβ) of the WT PTB RRM1 in free state (purple), in complex with SL UCUUU (red) and for the free state of the L151G mutant (blue). The experiments were acquired at 40°C for the WT protein in the free and SL UCUUU bound states, and at 25°C for the L151G mutant.