Table 1.
Substrate | Length, bases | Kdapp Cdc13p | Kdapp Cdc13 DBD |
---|---|---|---|
(TGTGTGGG)3 | 24 | 0.50 nM | 0.39 nM |
TGTGTGGGTGTG | 12 | 0.46 | 0.37 |
GTGGGTGTGTG | 11 | 0.46 | 0.37 |
TGTGGGTGTG | 10 | 55.0 | 48.0 |
caaGTGTGGGTGTGaac | 11 /17 | n.t. | 0.25 |
caaaTGTGGGTGTGaac | 10 /17 | n.t. | 12.0 |
caaaTGTGGGTGTaaac | 9 /17 | n.t. | 66.0 |
The apparent binding constant (Kdapp) for each substrate was determined from a compilation of three separate but identical gel shift experiments, each with a dilution series of protein and oligonucleotide concentration fixed at 20 pM. n.t., not tested.