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. 2014 Aug 4;2014:573936. doi: 10.1155/2014/573936

Table 2.

ssDNA binding properties of KpSSB, StSSB, PaSSB, KpSSBnStSSBc, and KpSSBnPaSSBc as analyzed by EMSA.

Protein DNA [Protein]50 (nM) Complex number
KpSSB dT20 ND 0
dT25 200 ± 20 1
dT35 220 ± 30 1
dT45 100 ± 10 1
dT50 110 ± 20 1
dT55 100 ± 20 2
dT60 100 ± 10 2

StSSB dT15 650 ± 120 1
dT20 450 ± 80 1
dT30 420 ± 60 1
dT40 420 ± 80 1
dT45 440 ± 60 2
dT50 440 ± 50 2

PaSSB dT20 ND 0
dT25 1700 ± 250 1
dT35 950 ± 180 1
dT45 780 ± 160 1
dT55 820 ± 90 1
dT60 810 ± 110 2
dT65 550 ± 70 2

KpSSBnStSSBc dT15 260 ± 60 1
dT20 110 ± 20 1
dT40 120 ± 20 1
dT45 160 ± 20 2

KpSSBnPaSSBc dT20 ND 0
dT25 390 ± 60 1
dT40 220 ± 30 1
dT55 230 ± 30 1
dT60 230 ± 30 2

[Protein]50 was calculated from the titration curves of EMSA by determining the concentration of the protein (μM) needed to achieve the midpoint value for input ssDNA binding. For some oligonucleotides, input ssDNA binding was the sum of the intensities from the two separate ssDNA-protein complexes. Errors are standard deviations determined by three independent titration experiments.