EC Number   |
General Stability |
Reference |
|---|
   3.1.31.1 | 2-O-alpha-mannosylglycerate protects against thermal denaturation, 0.5 M 2-O-alpha-mannosylglycerate increases Tm-value by 7.1°C. 0.5 M glycerol or trehalose increase the Tm-value by 0.8°C and 4.2°C, respectively |
665585 |
| 3.1.31.1 | correlation between the magnitude of protein stabilization and the restriction of fast backbone motions, mannosylglycerate restricts local motions in addition to the global motions of the protein. Unfolding/folding pathway remain undisturbed in the presence of mannosylglycerate but the solute shows a specific effect on the local motions of beta-sheet residues |
730894 |
| 3.1.31.1 | denaturation midpoint for urea is 1.5 M for mutant G20A, 1.1 M urea for mutant G20V, 0.82 Murea or mutant G20I and 2.0 M for wild-type enzyme |
664247 |
| 3.1.31.1 | denaturation of staphylococcal nuclease is induced by guanidinium hydrochloride, wild type and unlabeled mutant proteins are denatured in 20 mM Tris-HCl containing 0.1 M NaCl, pH 7.6 and 10 mM CaCl2, containing various concentrations of guanidinium hydrochloride at 25°C for 20 h to reach equilibrium |
705338 |
| 3.1.31.1 | enzyme tryptophan fluorescence spectra, fluorescence measurements of protein unfolding under pressure, high-pressure fluorescence spectroscopy and single value decomposition analysis, overview |
729277 |
| 3.1.31.1 | examination of acid-induced denaturation (monitored by intrinsic fluorescence of Trp140) measuring deltaG0H2O: D21N/T33V/T41I/S59A/P117G/A128A mutant: 9.5 kcal/mol, K9A mutant: 6.5 kcal/mol, Y91A mutant: 4.5 kcal/mol, Y91F mutant: 6.7 kcal/mol, Y93A mutant: 3.6 kcal/mol, Y93F mutant: 7.5 kcal/mol, E101A mutant: 8.4 kcal/mol, K127A mutant: 8.9 kcal/mol, A128S mutant: 8.2 kcal/mol. Examination of denaturation (monitored by intrinsic fluorescence of Trp140) with guanidinium chloride measuring the pH at the midpoint of the acid-induced unfolding: D21N/T33V/T41I/S59A/P117G/A128A mutant: 3.05, K9A mutant: 3.16, E73A mutant: 3.21, E75A mutant: 3.28, E75Q mutant: 3.27, D77A mutant: 3.31, Y91A mutant: 3.83, Y93A mutant: 4.10, E101A mutant: 3.14, K127A mutant: 2.94, A128S mutant: 3.20 |
699534 |
| 3.1.31.1 | native hairpin conformation is more stable than non-native conformation |
699852 |
| 3.1.31.1 | neural network-based prediction of mutation-induced protein stability changes |
666875 |
| 3.1.31.1 | no loss of activity during lyophilization |
135025 |
| 3.1.31.1 | perchlorate-denatured state has a very high content of secondary structure with no tertiary structure |
663763 |
