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. 2010 Aug;136(2):189–202. doi: 10.1085/jgp.200910374

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© 2010 Yusifov et al.

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Figure 5. — Tryptophan fluorescence reports WT- and D362/367A-RCK1 Ca²⁺ sensitivity. The intrinsic steady-state tryptophan fluorescence emission spectra of (A) WT and (B) D362/367A RCK1 recorded in increasing free [Ca²⁺]. As free [Ca²⁺] increases, the fluorescence intensity of WT-RCK1 decreases (A), whereas the fluorescence emission of D362/367A (B) shows no significant sensitivity to [Ca²⁺]. (C) The normalized fluorescence intensity at λ_330nm and free [Ca²⁺] = 0.00058 µM, plotted against free [Ca²⁺] for WT-RCK1 (red circles), D362/367A-RCK1 (blue triangles), and albumin (BSA) (black squares). The continuous curve is the least-squares fit to a Hill function, the parameters of which are shown in the panel. Errors represent standard errors of the mean.