Table 4. Comparison of the thermostability and hydrodynamic properties of Sp-DHDPS and Ec-DHDPS derived from circular dichroism spectroscopy and analytical ultracentrifugation studies.
| Enzyme | TMapp1 °C | s20,w (S) | Mr4 (kDa) | M (kDa) | f/f0 6 | a/b7 | KD42 (nM) |
|---|---|---|---|---|---|---|---|
| Sp-DHDPS | 72 | 7.22 | 135 | 1335 | 1.256 | 2.2 | 1.78 |
| Ec-DHDPS | 59 | 6.93 | 125 | 1283 | 1.263 | 2.6 | 763 |
1 The apparent melting temperature (T M app), or midpoint of the transition between folded and unfolded states, was determined from the ordinate maximum of a plot of the first derivative of the MRE as a function of temperature.
2 Value determined experimentally from the ordinate maximum of the c(s) distribution best-fit shown in Figure 4A.
3 Hydrodynamic properties reported in [34].
4 Molecular mass calculated from the amino acid sequence.
5 Value calculated experimentally from the apparent molecular mass taken from the ordinate maximum of the c(M) distribution best-fit shown in Figure 4B.
6 Frictional ratio calculated using the partial specific volume () method employing SEDNTERP software [53,54].
7 Axial-ratio as calculated from the program SEDNTERP using the method assuming a prolate ellipsoid.
8 The tetramer-dimer dissociation constant calculated from the global nonlinear least squares best-fit described in Figure 5