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. 2014 Mar 25;42(9):5949–5966. doi: 10.1093/nar/gku193

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© The Author(s) 2014. 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/3.0/), 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 7. — Relaxation and SAXS data of free and fas_16 RNA bound TIA-1-RRM2,3. (A) R₁ (top), R₂ (derived from R_1ρ, middle) and {¹H}-¹⁵N heteronuclear NOE values (bottom) of free (closed circles in black) and bound form (open circles in purple) measured at 298 K and pH 6.0 are shown. The average rotational correlation times (τ_c) for RRM2 and RRM3 in the RRM2,3 protein free (black) and bound to fas_16 (purple) are compared in (B). Residues in RRM3 helix α0 are highlighted with an orange box. (C) SAXS data of TIA-1-RRM2,3 free (black) and bound to fas_16 RNA (purple) and (D) the corresponding pairwise distribution functions.