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. 2015 Feb 10;43(4):2400–2411. doi: 10.1093/nar/gkv072

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© The Author(s) 2015. 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-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 5. — NMR chemical shift perturbations of Hfq by A_us and A_ds. Hfq65 R16A/R17A protein (0.1 mM) were titrated with A_us and A_ds, respectively. (A) Selected regions of ¹H-¹⁵N HSQC spectra of Hfq upon A_us (left) and A_ds (right) titration. (B) Chemical shift differences between the first and last titration points for A_us and A_ds are presented as green and red column bars, respectively. (C, E) Both A_us and A_ds binding to Hfq result in prominent chemical shift perturbations on the distal side of Hfq. (D, F) Residues Q8, Q41 and V43 on the proximal side of Hfq are also perturbed by A_us and A_ds titration. Hfq is colored according to chemical shift changes using a blue to red gradient. The resonances of F42 and H57, which disappeared upon A_us and A_ds titration, are colored purple. Unassigned residues are colored dark blue.