Snail NSCaTE<sub>LCav1</sub> and mammalian NSCaTE<sub>Cav1.2</sub> peptides assume an alpha-helix upon binding calmodulin (CaM).

<p>(A) 17 mer NSCaTE and 21 mer IQ peptide sequences are used in circular dichroism (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0061765#pone-0061765-g006" target="_blank">Figures 6</a>) and Gel Shift Mobility Assays (<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0061765#pone-0061765-g007" target="_blank">Figures 7</a>). (B,C) Differential spectra of NSCaTE peptide indicate a helical transformation with snail and mammalian NSCaTE upon addition of the helix stabilizing agent, trifluoroethanol (TFE: dashed line; no TFE: solid line, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0061765#pone-0061765-g006" target="_blank">Figure 6B</a>) or upon addition to CaM (solid line = 1∶1 CaM:peptide, dashed line = 1∶2 CaM:peptide, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0061765#pone-0061765-g006" target="_blank">Figure 6C</a>). Each trace is obtained by subtracting the 10 µM CaM-alone trace from the corresponding NSCaTE+CaM spectrum. Y axis units are mean residue ellipticity or (θ), (difference in spectra corrected for total protein/peptide concentration).</p>