Table 1.
Apparent liposome affinities of Ca2+-saturated Syt7 and Syt1 C2 domain fragments
| Protein fragment | KD (µM) | SD | h | SD |
| Syt7 C2A | 2.40 | 0.54 | 2.18 | 0.41 |
| Syt7 C2B | 34.97 | 2.92 | 1.02 | 0.09 |
| Syt7 C2A*B | 4.12 | 0.80 | 3.1 | 0.52 |
| Syt7 C2A*b | 4.29 | 0.18 | 1.74 | 0.26 |
| Syt7 C2aB* | 8.06 | 0.39 | 2.03 | 0.26 |
| Syt7 C2A F167M,R231K | 8.68 | 0.44 | 1.61 | 0.17 |
| Syt1 C2A | 551.1 | 134.26 | 1.34 | 0.159 |
| Syt1 C2B | 637.37 | 146.89 | 1.78 | 0.38 |
| Syt1 C2A*B | 24.05 | 1.77 | 2.15 | 0.46 |
| Syt1 C2A*b | 245.5 | 4.49 | 1.95 | 0.24 |
| Syt1 C2aB* | 267.23 | 38.96 | 2.09 | 0.25 |
| Syt1 C2A M173F,K236R | 95.48 | 25.9 | 1.51 | 0.3 |
The listed apparent KDs and Hill coefficients (h), as well as their SDs, were obtained from fitting the FRET data obtained in liposome titrations of the indicated Ca2+-saturated Syt7 and Syt1 C2 domain fragments. At least three titrations were performed for each fragment. KDs and h values were derived for each titration, and the averages as well as SDs were calculated. The protein concentrations were 20 nM for all Syt7 fragments and 100 nM for all Syt1 fragments.