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. Author manuscript; available in PMC: 2016 Feb 27.
Published in final edited form as: J Mol Biol. 2014 Sep 16;427(4):824–839. doi: 10.1016/j.jmb.2014.09.002

Table 1.

Summary of results.

WH2
Constructs
ΔrGd(kJ/mol) Kd(µM) Elongation
rate (sub/s)
max rate
at 3µM (a.u.)
ΔrGdf
(kJ/mol)
Kdf(µM) Inhibition
of nucleation
Sa −0.3 ± 0.3 1.14 1.5 ± 0.2 4.1 ± 0.5 N/D 28 +++
Sb 5.9 ± 0.3 0.09 6.5 ± 0.7 3.5 ± 0.4 −8 ± 3 N/D ++
Sc 3.9 ± 0.1 0.21 (0.01) 6.6 ± 1.3 3.2 ± 0.4 −1.6 ± 0.3 2.0
Sd 1.2 ± 0.1 0.62 (0.03) 6.3 ± 0.5 3.1 ± 0.1 −6.2 ± 0.6 13 +++
Cs3 5.4 ± 0.3 0.11 N/D 4.0 ± 0.3 −0.9 ± 0.5 1.4 ++
S3d 0.6 ± 0.2 0.78 N/D 5.2 ± 0.7 −15 ± 5 500 +
Sc[qe] 4.6 ± 0.2 0.15 N/D 2.1 ± 0.2 −1.6 ± 0.4 1.9 +++
Na 0.7 ± 0.1 0.75 N/D 3.0 ± 0.3 ## ## ++
Na[fs] * * N/D 5.5 ± 0.4 N/D N/D

The values in parentheses are the predicted Kd’s for a second actin monomer binding to Sc3d as described for Figure 3B.

*

Na[fs] affinity is too weak to determine with confidence. It is > 30 µM.

##

Regression for Na with Kdf free did not converge.

N/D = not determined.