. 2020 Aug 18;3(5):883–895. doi: 10.1021/acsptsci.0c00054

Table 2. Summary of Photoswitchable NAM Affinities and B_max Estimates under Different Light Conditions as Determined by MS Binding Assays^a.

	Dark		500 nm		380 nm
Allosteric ligand	pK_D^b	B_max (pmol/mg protein)^c	pK_D^b	B_max (pmol/mg protein)^c	pK_D^b	B_max (pmol/mg protein)^c
Alloswitch-1	7.51 ± 0.04	71.52 ± 6.89	7.47 ± 0.07	76.34 ± 13.98	7.03 ± 0.05****	35.06 ± 11.68
MCS0331	7.85 ± 0.03	92.84 ± 9.92	7.58 ± 0.06*	151.51 ± 16.28	6.90 ± 0.10****	21.06 ± 2.05

Data sets were analyzed according to eq 2 in the Supporting Information. Difference in equilibrium dissociation constants of allosteric ligands under different light conditions were determined by one-way ANOVA and Tukey post hoc test where appropriate. *, P < 0.1, and ****, P < 0.0001 vs dark conditions.

Negative logarithm of the allosteric modulator equilibrium dissociation constant.

Receptor expression of hmGlu₅.

Table 2. Summary of Photoswitchable NAM Affinities and Bmax Estimates under Different Light Conditions as Determined by MS Binding Assaysa.

Table 2. Summary of Photoswitchable NAM Affinities and B_max Estimates under Different Light Conditions as Determined by MS Binding Assays^a.