. Author manuscript; available in PMC: 2018 Jan 1.

Published in final edited form as: Biochim Biophys Acta. 2016 Oct 21;1864(1):31–38. doi: 10.1016/j.bbamcr.2016.10.011

Table 1. Parameters describing EphA2 unliganded dimerization.

The dissociation constants K_diss and the dimerization free energies, ΔG, for EphA2, EphA2ΔSAM, L223R/L254R/V255R EphA2, and L223R/L254R/V255R EphA2ΔSAMThe differences in dimer stability due to SAM domain deletion (ΔΔG_SAM) and due to the L223R/L254R/V255R mutations (ΔΔG_LLV), are also shown.

	K_diss (rec/μm²)	ΔG (kcal/mole)	ΔΔG_SAM	ΔΔGLLV
EphA2	206 ± 73	−5.03 ± 0.25
EphA2ΔSAM	47 ± 13	−5.90 ± 0.17	−0.9 ± 0.3
L223R/L254R/V255R EphA2	1100 ± 482	−4.03 ± 0.33		1.0 ± 0.4
L223R/L254R/V255R EphA2ΔSAM	343 ± 80	−4.72 ± 0.17	−0.7 ± 0.4	1.2 ± 0.2