TABLE 1.
The set of proteins studied ranked according to the unfolding force measured experimentally and according to the unfolding rate estimated in the simulations with the two different models
| Class | Experiment | Ref. | Gō | τunfold (ps) | EEF1 | τunfold (ps) |
|---|---|---|---|---|---|---|
| Hard | Ubiquitin (N-C) 203 ± 35 pN at 400 nm s−1 | (11) | Protein L | 5.0 × 106 | Protein L | 2.9 × 104 |
| I27 204 ± 26 pN at 400–600 nm s−1 | (2) | Ubiquitin (N-C) | 1.7 × 105 | Ubiquitin (N-C) | 3.0 × 103 | |
| Protein L 152 ± 5 pN at 700 nm s−1 | (5) | I27 | 1.8 × 104 | Ubiquitin (C-48) | 1.6 × 103 | |
| I27 | 520 | |||||
| Intermediate | E2lip3 (N-41) 177 ± 3 pN at 700 nm s−1 | (4) | E2lip3 (N-41) | 1.4 × 103 | Tenascin | 29 |
| Tenascin 137 ± 12 pN at 200–600 nm s−1 | (53) | Tenascin | 340 | E2lip3 (N-41) | 21 | |
| Ubiquitin (C-48) 85 ± 20 pN at 300 nm s−1 | (11) | Ubiquitin (C-48) | 90 | |||
| Soft | Spectrin 25-35 pN at 300 nm s−1 | (6) | Spectrin | 54 | E2lip3 (N-C) | 4.9 |
| E2lip3 (N-C) <15 pN at 600 nm s−1 | (4) | E2lip3 (N-C) | 47 | Spectrin | 1.9 |
Although the exact order is different, the three methods rank the proteins in the same three classes of mechanical resistance (with one exception, ubiquitin (C-48) which is found to be “hard” with the EEF1 model).