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. 2016 Jun 30;11(1):34–45. doi: 10.1080/19336950.2016.1207023

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© 2017 The Author(s). Published with license by Taylor & Francis

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 3. — Effects of IVS3-S4 on Ca_V1.3 activation are correlated with the number of glycine residues of the linker. (A) Summary of V_1/2 for various α_1D channels including the native forms and chimeric mutants. These channel constructs were also named according to the number of glycines (G_X) within the linker. *, p < 0.05 and ***, p < 0.001. (B) Flexibility of different G_X linkers affected the kinetics of channel activation. At −30 mV, time constant (τ) values of current traces were fitted, as shown by the exemplars of G₀ and G₁₉ (upper), and summarized for voltages from −30 mV to +10 mV (lower). (C and D) Correlations between the linker flexibility (G_X) and voltage-dependence (V_1/2) or time-dependence (τ, at −30 mV) of activation. The red lines are visually appended to illustrate the trends in relation to G_X and loop flexibility.