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Shifts in the R3 equilibrium induced by binding of autocamtide-2 (AC-2). EPR spectra for site 307 show that the level of the mobile spectral component arising from undocked conformation of the R3 segment increases in the presence of AC-2. The T286E mutation increases the affinity of this interaction as evidenced by the lower molar ratio of peptide to CaMKII (x axis) required to increase the mobile spin label fraction.
