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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
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Cell Communication and Signaling

ISSN: 1478-811X