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. Author manuscript; available in PMC: 2013 Oct 26.
Published in final edited form as: J Mol Biol. 2012 Jul 21;423(3):365–385. doi: 10.1016/j.jmb.2012.07.011

Table 1.

Dissociation constants of Ca2+ and TRTK-12 from Ca2+-S100B or Ca2+-S100B-target complexesa

Ca EF2KD (µM)b Ca EF2 + TRTKKD (µM)c TAMRA-TRTKKD (µM)d TRTKKD (µM)e
S100B 56 ± 9 (5)f 12 ± 10 (5)g 1.2 ± 0.2 (2)g 2.9 ± 0.5 (2)g
D61NS100B 412 ± 67 (3) 29 ± 1.2 (3) 1.4 ± 0.2 (2) 2.1 ± 0.7 (2)
D63NS100B 50 ± 8.6 (3) 10 ± 2.2 (4) 0.47 ± 0.04 (2) 3.7 ± 0.3 (2)
D65NS100B 968 ± 171 (3) 73 ± 4.4 (3) 0.34 ± 0.16 (2) 1.6 ± 0.4 (2)
E72AS100B 471 ± 133 (4) 18 ± 3.7 (4) 0.33 ± 0.11 (2) 4.8 ± 1.1 (2)
a

Values in parenthesis are the number of experiments performed.

b

Dissociation constants of Ca2+ from the tight site (EF2) of S100B and S100B mutants; Ca EF2KD = [S100B][Ca2+]/[S100B-Ca2+]EF2

c

Dissociation constants of Ca2+ from the tight site (EF2) of S100B and D63NS100B in the presence of TRTK-12 peptide.

d

Dissociation constants of TAMRA-TRTK-12 from Ca2+-S100B and Ca2+- D63NS100B as measured directly from fluorescence polarization.

e

Dissociation constants of TRTK-12 from Ca2+-S100B as measured from competition experiments with TAMRA-TRTK-12.

f

Values reported by Rustandi et al.14

g

Values reported by Charpentier et al.7