Parameters describing the stability and structure of EphA2 unliganded dimers
Kdiss is the dissociation constant (receptors/μm2); ΔG is the dimerization free energy; Ẽ is the intrinsic FRET efficiency; and d is the calculated distance between the fluorescent proteins in the EphA2 dimers. Kdiss and Ẽ are determined from the fit of the dimerization model to the FRET data, and the uncertainties are the 95% confidence intervals from the fit. ΔG and d are calculated using Equations 1 and 2, respectively.