. Author manuscript; available in PMC: 2013 Sep 11.

Published in final edited form as: Biochemistry. 2012 Aug 29;51(36):7189–7201. doi: 10.1021/bi300865g

Table 4.

Summary of the kinetic properties of S100B binding to p53, TRTK12, NDR, HDM2 and HDM4 and determined using NMR experiments and LineShapeKin analysis.

Peptide	K_{d, App} (μM)^a	K_off (s^-1)	K_on (1×10⁷ M^-1 s^-1)
TRTK12	1.0 ± 0.5	100 ± 20	10 ± 4
p53, low salt	1.0 ± 0.5	1000 ± 200	100 ± 40
p53, high salt	10 ± 2	1000 ± 200	10 ± 2
NDR	n.a.^b	n.a.^b	n.a.^b
HDM2	0.1 ± 0.02^c	100 ± 20	100 ± 40
HDM4	1.0 ± 0.5^c	10 ± 2	1.0 ± 0.4

Peptide binding was fit to a single site model for all peptides during the LineShapeKin analysis. All reported values are for the apparent K_d.

K_d values and kinetic rates could not be solved for analytically. See Methods and Table 1.

Binding model used was one peptide per S100B dimer. K_d and K_off is taken directly from 2D matrix.