. 2017 Feb 23;7:42760. doi: 10.1038/srep42760

Table 1. K_d values for binding of the E2·E3BP-derived domains to PDK1-PDK4 as detected by fluorescence spectroscopy.

Kd (μM)	DANS-L1	DANS-L2S	DANS-L1L2S MS1	DANS-L1L2S MS2	DANS-L3S’	Dapoxyl-L3S’
PDK1	4.43 ± 0.35	17.14 ± 0.94	2.10 ± 0.12	3.62 ± 0.25	No binding	No binding
PDK2	0.91 ± 0.08	1.38 ± 0.03	0.89 ± 0.09	0.64 ± 0.09	0.025^a	2.07 ± 0.06
PDK3	0.62 ± 0.03	1.21 ± 0.06	0.54 ± 0.05	0.396 ± 0.06	0.103^a	No binding
PDK4	0.35 ± 0.06	2.07 ± 0.16	0.27 ± 0.02	0.397 ± 0.03	5.93 ± 1.06	5.02 ± 0.13

^aOn binding of PDK2 and PDK3 to DANS-L3S’, quenching of the DANS-L3S’ fluorescence was observed while in others enhancement resulted. See SI Experimental Procedures for details.

Table 1. Kd values for binding of the E2·E3BP-derived domains to PDK1-PDK4 as detected by fluorescence spectroscopy.

Table 1. K_d values for binding of the E2·E3BP-derived domains to PDK1-PDK4 as detected by fluorescence spectroscopy.