Table 2 Structural features of the different lipases variants in aqueous conditions.
From: Insight into the molecular mechanism behind PEG-mediated stabilization of biofluid lipases
Enzyme | T a(K) | RMSD (nm) | Radius of Gyration (nm) | Secondary Structure (# of Residues) | SASA (nm) | |
|---|---|---|---|---|---|---|
SCb | Main chain + H | |||||
RML | 298 | 0.15 ± 0.03 | 1.71 ± 0.01 | 176 ± 5 | 100 ± 1 | 16.6 ± 0.2 |
348 | 0.26 ± 0.01 | 1.71 ± 0.01 | 172 ± 4 | 100 ± 1 | 17.0 ± 0.1 | |
368 | 0.29 ± 0.03 | 1.72 ± 0.01 | 167 ± 3 | 100 ± 1 | 17.3 ± 0.1 | |
cRML60 | 298 | 0.14 ± 0.02 | 1.70 ± 0.01 | 182 ± 8 | 121 ± 7 | 14.5 ± 2.2 |
348 | 0.22 ± 0.01 | 1.71 ± 0.01 | 172 ± 3 | 121 ± 6 | 15.2 ± 2.3 | |
368 | 0.27 ± 0.03 | 1.72 ± 0.01 | 170 ± 2 | 122 ± 7 | 15.2 ± 2.3 | |
cRML60-S2 | 298 | 0.15 ± 0.02 | 1.72 ± 0.01 | 176 ± 2 | 121 ± 4 | 14.4 ± 0.7 |
348 | 0.20 ± 0.02 | 1.73 ± 0.02 | 174 ± 7 | 126 ± 4 | 15.1 ± 1.1 | |
368 | 0.25 ± 0.03 | 1.74 ± 0.01 | 169 ± 2 | 128 ± 2 | 15.9 ± 0.6 | |
cRML60-S7 | 298 | 0.12 ± 0.01 | 1.70 ± 0.01 | 183 ± 1 | 123 ± 1 | 14.0 ± 0.5 |
348 | 0.21 ± 0.01 | 1.72 ± 0.01 | 173 ± 3 | 126 ± 1 | 15.3 ± 1.4 | |
368 | 0.21 ± 0.01 | 1.72 ± 0.01 | 174 ± 6 | 126 ± 3 | 15.5 ± 2.8 | |
