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Triadin<sup>200–232</sup> and triadin<sup>200–231</sup> peptides bind to RyR1 and exhibit a disordered secondary structure.

By Elize Wium (310325), Angela F. Dulhunty (202327) and Nicole A. Beard (310326)


<p>(A) Circular dichroism spectra averaged from four scans and corrected for the 10 mM sodium phosphate buffer are shown. Both triadin peptides (triadin<sup>200–231</sup> (black trace) and triadin<sup>200–232</sup> (grey trace); 0.03 mg/ml) show a negative peak at ∼197 nm, consistent with an intrinsically disordered structure. A positive peak at ∼190 nm and negative peaks at ∼208 and ∼223 nm (indicative of α-helical secondary structure) or a positive peak at ∼195 nm and a negative peak at ∼217 nm (indicative of β-sheet secondary structure), are absent. (B) Western blot, following streptavidin-agarose affinity chromatography, showing the association of RyR1 with biotin tagged triadin peptide. The upper half of the membrane was probed with anti-RyR1 antibody and the lower half was probed with Streptactin-HRP conjugate to identify the biotin tagged peptides. <i>Lane 1</i> protein sample eluted from streptavidin-agarose incubated with RyR1 alone; <i>Lane 2</i> purified RyR1 alone (control); <i>Lane 3</i> biotin tagged triadin<sup>200–231</sup> peptide alone (control); <i>Lanes 4 and 5</i> protein sample eluted from streptavidin-agarose affinity chromatography, where streptavidin-agarose was incubated with biotin tagged triadin<sup>200–232</sup> or triadin<sup>200–231</sup> peptide respectively, prior to incubation with RyR1.</p

Topics: Biochemistry, Physiology, peptides, ryr1, disordered
Year: 2013
DOI identifier: 10.1371/journal.pone.0043817.g001
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Provided by: FigShare
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