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. Author manuscript; available in PMC: 2017 Oct 11.
Published in final edited form as: J Chem Theory Comput. 2016 Sep 9;12(10):4717–4725. doi: 10.1021/acs.jctc.6b00150

Figure 7.

Figure 7

Structural studies of T202L and F200A mutant of TIS11d. 15N-1H HSQC spectra (A) of TIS11d wild type (black), T202L (blue) and F200A (red) mutants of TIS11d. On top, a schematic representation of the RNA-binding domain depicts the ZFs as rectangles and the linker region as a line. The circles indicate residues along the primary sequence with a cross-peak in the 15N-1H HSQC spectrum. Black box indicates the α-helix in ZF2. The F200A mutant protein is less stable than the wild type protein as indicated by the presence of degradation peaks in the region between 7.8 and 8.2 ppm in the 1H dimension and 125 and 130 ppm in the 15N dimension. Circular dichroism spectra (B) of TIS11d wild type (black), T202L (blue) and F200A (red) mutants of TIS11d and TTP (gray).