TABLE 1.
Thermodynamic parameters determined from ITC measurements
| Constructs | KD (µM) | n | ΔH (kcal/mol) | ΔG (kcal/mol) | −TΔS (kcal/mol) |
|---|---|---|---|---|---|
| hnRNPA1(1–249)–5BSL3.2 | 0.286 ± 0.063 | 1.29 ± 0.18 | −23.03 ± 6.15 | −8.94 ± 0.14 | 14.13 ± 6.00 |
| hnRNPA1(1–196)–5BSL3.2 | 0.243 ± 0.030 | 0.99 ± 0.13 | −37.5 ± 6.29 | −9.03 ± 0.08 | 28.47 ± 6.23 |
| hnRNPA1(11–88)–5BSL3.2 | 2.08 ± 0.19 | 1.53 ± 0.13 | −31.6 ± 5.29 | −7.76 ± 0.05 | 23.87 ± 5.32 |
| hnRNPA1(89–179)–5BSL3.2 | 2.48 ± 0.48 | 2.44 ± 0.10 | −15.83 ± 7.81 | −7.66 ± 0.12 | 8.2 ± 7.93 |
| hnRNPA1(1–196)–5BSL3.2Apical stem–loop | 0.128 ± 0.006 | 0.97 ± 0.09 | −31.6 ± 5.95 | −9.41 ± 0.03 | 22.2 ± 5.94 |
| hnRNPA1(1–196)–linear 12 nt loop | 0.224 ± 0.013 | 0.93 ± 0.08 | −20.2 ± 3.43 | −9.07 ± 0.04 | 11.08 ± 3.41 |
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This table summarizes the binding parameters derived from isothermal titration calorimetry (ITC) experiments examining the interactions between various hnRNPA1 constructs specifically UP1 with 5BSL3.2 RNA and between hnRNPA1 (residues 1–196) and different RNA constructs. Listed parameters include the dissociation constant (KD), binding stoichiometry (N), enthalpy change (ΔH), entropy contribution (TΔS), and Gibbs free energy change (ΔG). Data are expressed as the mean ± standard deviation from a minimum of three independent experiments.
