Table 2.
Biophysical characterizations of Tbab proteins
| % Secondary Structures | Aggregation State |
Binding Affinity (ITC KD/μM) |
Binding Affinity (SPR KD/μM) |
|
|---|---|---|---|---|
| Tbab1‐1 | 90 | 0.89 | n. a. | 62.7 ± 6.5 |
| Tbab1‐2 | 0 | n. a. | n. a. | n. a. |
| Tbab1‐3 | 100 | 1.15 | n. a. | n. a. |
| Tbab1‐4 | 84 | 1.02 | 21.2 ± 1.1 | 3.2 ± 0.9 |
| Tbab1‐5 | 97 | 2.15 | n. a. | n. a. |
| Tbab1‐6 | 100 | 2.06 | n. a. | n. a. |
| Tbab1‐7 | 55 | 1.14, 0.91 | 39.2 ± 2.8 | 0.85 ± 0.08 |
| Tbab1‐8 | 69 | 0.94 | 25.8 ± 3.5 | 0.96 ± 0.06 |
| Tbab1‐9 | 49 | 1.14, 0.91 | 32.9 ± 3.8 | 3.8 ± 0.6 |
| Tbab2‐4 | 54 | 1.01 | 7.2 ± 0.8 | 0.36 ± 0.05 |
The secondary structural content was measured with CD using the CD signal of DS119 as the reference (100%). The aggregation state was determined by analytical size exclusion chromatography. The binding affinity was determined by SPR. n. a., not available