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Table 2 Monomer-dimer equilibrium constants for wild type CASKIN2 SAM1-SAM2 and an oligomerization-inhibited double (G537D/K540E) at two NaCl concentrations

From: A new mode of SAM domain mediated oligomerization observed in the CASKIN2 neuronal scaffolding protein

  150 mM NaCl 300 mM NaCl
Wild type   
K d (μM) 52.9 (49.3, 56.5) 27.6 (26.8, 28.3)
 φ (monomer) 1.25 1.27
 φ (dimer) 1.28 1.25
G537D/K540E   
K d (μM) n.d. 99.8 (98.9,100.7)
 φ (monomer) 1.14 1.02
  1. Values in parentheses represent the 95 % confidence intervals obtained from a genetic-algorithm Monte Carlo analysis. φ represents the anisotropy of the molecule, with a value close to 1.0 indicating a more compact and globular structure, while increasingly larger values reflect more extended shapes. Since the dimer concentration of the G537D/K540E mutant is negligible, the anisotropy of the dimer was not calculated. A K d for the G537D/K540E mutant at 150 mM NaCl could not be detected (n.d.) because the sample was essential monomeric