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. 2018 Dec 14;11:459. doi: 10.3389/fnmol.2018.00459

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Copyright © 2018 Tsvetkov, Roman, Baksheeva, Nazipova, Shevelyova, Vladimirov, Buyanova, Zinchenko, Zamyatnin, Devred, Golovin, Permyakov and Zernii.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Calcium, magnesium and zinc dependences of thermal stability of NCS-1. Mid-transition temperatures of NCS-1 (25 μM) denaturation determined form tryptophan fluorescence at 350/330 nm (I₃₅₀/I₃₃₀) for apo (A), Mg²⁺-saturated (B), Ca²⁺-saturated (E), or Zn²⁺-saturated (F) protein in the presence of increasing concentrations of the alternative cations. Mid-transition temperatures of NCS-1 (25 μM) aggregation determined form light scattering at 350 nm for apo (C), Mg²⁺-saturated (D), Ca²⁺-saturated (G), or Zn²⁺-saturated (H) protein in the presence of increasing concentrations of the other cations.