. Author manuscript; available in PMC: 2021 Jul 30.

Published in final edited form as: Biochemistry. 2020 May 4;59(20):1946–1960. doi: 10.1021/acs.biochem.0c00320

Table 2.

Dissociation constants (K_D) for DnaK binding to KLR-70 and KLR-70-C-AF488.

Peptide	Method	K_D

KLR-70	Direct binding (native gels)	158 ± 73 nM ^(*)
KLR-70	Competitive binding (fluorescence anisotropy)	890 ± 390 nM ^(*)
KLR-70-C-AF488	Direct binding (fluorescence anisotropy)	1.73 ± 0.37 μM

^(*)

Differences in K_D determined for KLR-70 binding DnaK by gel-shift and anisotropy assays are not statistically significant (p = 0.15) when analyzed using a two-tailed T-test assuming unequal variances and using a 95% confidence interval cutoff.