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The binding affinity of 1-anilinonaphthalene-8-sulfonic acid (ANS) to the gap-closed variant was measured using a Shimadzu RF-5301 fluorescence spectrometer. The change of ANS fluorescence intensity with protein concentration (F(x)) was fitted to a one-site binding model, as follows:
where L0 is the total ANS concentration (1 μM), x is the total protein concentration, Kd is the dissociation constant, and ΔA is the difference of fluorescence intensities between the protein-free and protein-bound ANS.
Copyright and License information: ©2019 Biophysical Society.
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