. Author manuscript; available in PMC: 2020 May 1.

Published in final edited form as: J Struct Biol. 2019 Mar 14;206(2):193–203. doi: 10.1016/j.jsb.2019.03.003

Table 6.

Binding affinities of PAM-derived peptides to hPg

Peptides	T (° C)	K_d (kinetics)^a (nM)	K_d (steady state)^b (nM)
AGL55_NS88.2	15	160 ± 5	350 ± 2
	25	630 ± 11	830 ± 45
	37	n.d.^c	7,100 ± 500
KTI55_SS1448	15	360 ± 13	540 ± 22
	25	2,100 ± 160	1,500 ± 110
	37	n.d.^c	27,000 ± 640
VEK75_AP53	15	n.d.^d	n.d.^d
	25	0.7 ± 0.2	n.d.^d
	37	15 ± 7	45 ± 18
VEK75_{AP53_RH1/AA}	15	26 ± 1	n.d.^e
	25	50 ± 5	82 ± 12
	37	n.d.^c	890 ± 77

Dissociation constants (K_d) were calculated from k_off/k_on. All data were collected from triplicate runs and are presented as the mean ± S.D.

Dissociation constants (K_d) were calculated from steady state plots of the peak value in the association stage vs concentration of peptides. All data were collected from triplicate runs and are presented as the mean ± S.D.

k_off rates were too fast for accurate kinetic assessment.

Binding was too tight to be accurately measured.

Optimal measurements were made by kinetic binding methods.