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. 2013 Sep 25;3:398–405. doi: 10.1016/j.fob.2013.09.006

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© 2013 The Authors

This is an open-access article distributed under the terms of the Creative Commons Attribution-NonCommercial-No Derivative Works License, which permits non-commercial use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig. 2 — The W(−1)A/P75A double mutant does not undergo complete Ca²⁺-induced conformational change. (A) The CD spectra of the wild-type ScaADoc (dashed line) and W(−1)A/P75A (dotted line) proteins showcase how complete abrogation of the clasp interaction interferes with the folding of the molecule in the presence of Ca²⁺. (B) Overlay of the 2D ¹H–¹⁵N HSQC spectra of the Ca²⁺-bound (red) and apo-form (black) of the double mutant, W(−1)A/P75A-ScaADoc, wherein the divalent metal cation has little effect on its tertiary structure. (For interpretation of the references to colour in this figure legend, the reader is referred to the web version of this article.)