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Glutamate dehydrogenase (GDH) from Thermus thermophilus is a homotrimeric enzyme that tends to dissociate at acidic pH values.
The hydrate slurry thus formed is depressurized to dissociate at a lower temperature, typically 5 9 °C, thereby absorbing heat from a space to be refrigerated.
Variable temperature FTIR demonstrated that hydrogen bonds completely dissociate at around 170 °C for polyurethanes chain extended by HQEE compared to around 110 °C for their TD analogs.
These complexes being located on the graphene edges are stable at low temperatures but irreversibly dissociate at temperatures above 50 60 K.
The backbone of the polymer linked by amide bond and abundant of carboxyl groups as pendant group could form strong intermolecular and intramolecular hydrogen bond at lower temperature and dissociate at higher temperature, resulting in the polymer with thermo-sensitivity.
This indicates that proteins need to be able to rapidly associate and dissociate at specific moments of the cell cycle; these data are supported by observations in other organisms such as C. crescentus, where PBP2 was shown to associate to the cell wall synthesis machinery dynamically and transiently10.
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Consequently, larger amounts of hydrate were dissociated at higher temperatures.
Adherent cells were dissociated at the indicated times with 0.05% trypsin-EDTA and then counted by trypan blue dye exclusion.
While about 7.5 mol% of hydrate formed in pure water dissociated at similar condition.
Interestingly, an increase in inhibitor concentration decreased the amount of gas hydrate that dissociated at the equilibrium temperature.
A significant fraction of these cluster ions can be dissociated at activation energies lower than the threshold for peptide fragmentation.
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