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. Author manuscript; available in PMC: 2012 Oct 28.

Published in final edited form as: J Mol Biol. 2011 Sep 8;413(3):712–725. doi: 10.1016/j.jmb.2011.08.059

(a) 2D ¹H-¹⁵N HSQC spectral overlay of ¹⁵N-labeled Act-EF34 in the absence (black) and presence of bound WT palladin peptide (magenta). (b) Chemical shift perturbation of Act-EF34 amide resonances upon complex formation with either titin Zr7 (gray) or palladin peptide (magenta). The α-helical regions or β-strands of Act-EF34 are designated by filled or open bars, respectively, above the plot. Also indicated (dotted line) is the chemical shift cut-off value used for the definition of AIRs as input for the HADDOCK calculations (0.17 ppm).

(a) 2D ¹H-¹⁵N HSQC spectral overlay of ¹⁵N-labeled Act-EF34 in the absence (black) and presence of bound WT palladin peptide (magenta). (b) Chemical shift perturbation of Act-EF34 amide resonances upon complex formation with either titin Zr7 (gray) or palladin peptide (magenta). The α-helical regions or β-strands of Act-EF34 are designated by filled or open bars, respectively, above the plot. Also indicated (dotted line) is the chemical shift cut-off value used for the definition of AIRs as input for the HADDOCK calculations (0.17 ppm).