TABLE 3.
Dissociation constants for PTB1 constructs: GABA RNAs complexes
Protein | I | I34 | I11 | I11/E |
PTB1 |
KD1 = 5 ± 1 nM, n1 = 2 KD2 = 130 ± 5 nM, n2 = 1 |
KD1 = 2 ± 1 nM, n1 = 1 KD2 = 30 ± 5 nM, n2 = 1 |
KD = 15 ± 2 nM, n = 1.5 |
KD1 = 30 ± 5 nM, n1 = 0.5 KD2 = 100 ± 15 nM, n2 = 1.5 |
PTB1:12 |
KD1 = 50 ± 5nM, n1 = 1 KD2 = 300 ± 20 nM, n2 = 1 |
KD1 = 50 ± 7 nM, n1 = 1 KD2 = 160 ± 10 nM, n2 = 1.5 |
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PTB1:34* |
KD1 = 40 ± 5 nM, n1 = 1.5 KD2 = 150 ± 10 nM, n2 = 3 |
KD = 50 ± 3 nM, n = 3 |
KD1 = 10 ± 3 nM, n1 = 0.5 KD2 = 50 ± 5 nM, n2 = 1 KD3 = 1 mM, n3 = 2.5 |
Data were obtained by allowing both n and K to vary simultaneously. (*) The values for I11/E are approximate, since resolution of individual bands in the gel was difficult. Only one band was observed for I11; 100 mM NaCl, 1 mM MgCl2, 10 mM sodium cacodylate (pH 7), 20 μg/mL BSA, 10 μg/mL tRNA, 4° C.