AbstractTwo recent papers comparing the structure of a hyperthermophilic protein with its mesophilic counterpart both conclude that large networks of ion-pairs are important for hyperthermostability. How and why is not yet clear
Enzymes from thermophilic and, particularly, from hyperthermophilic organisms are surprisingly stabl...
Enzymes from thermophilic and, particularly, from hyperthermophilic organisms are surprisingly stabl...
Background Thermophilic proteins sustain themselves and function at higher temperatures. Despite the...
We used classical molecular dynamics simulation method to investigate physical factors responsible f...
Studies of the structural basis of protein thermostability have produced a confusing picture. Small ...
Protein folding is governed by a variety of molecular forces including hydrophobic and ionic interac...
Organisms that thrive under extreme conditions, such as high salt concentration, low pH, or high tem...
AbstractCold shock proteins (Csps) from mesophiles and thermophiles differ widely in their stabiliti...
AbstractBackground: The hyperthermophile Pyrococcus furiosus is one of the most thermostable organis...
In this study the structural and thermodynamic basis of the thermal stability of proteins has been s...
SummaryDespite numerous studies, understanding the structural basis of protein stability in thermoph...
The boiled enzyme was toppled as a standard enzymology control when researchers in the 1970s started...
AbstractWe found that the CutA1 protein, from Pyrococcus horikoshii (PhCutA1), has an extremely high...
Biochemical, crystallographic, and computational data support the hypothesis that electrostatic inte...
The bases of the hyperthermostability of rubredoxin from Pyrococcus furiosus (RdPf) have been probed...
Enzymes from thermophilic and, particularly, from hyperthermophilic organisms are surprisingly stabl...
Enzymes from thermophilic and, particularly, from hyperthermophilic organisms are surprisingly stabl...
Background Thermophilic proteins sustain themselves and function at higher temperatures. Despite the...
We used classical molecular dynamics simulation method to investigate physical factors responsible f...
Studies of the structural basis of protein thermostability have produced a confusing picture. Small ...
Protein folding is governed by a variety of molecular forces including hydrophobic and ionic interac...
Organisms that thrive under extreme conditions, such as high salt concentration, low pH, or high tem...
AbstractCold shock proteins (Csps) from mesophiles and thermophiles differ widely in their stabiliti...
AbstractBackground: The hyperthermophile Pyrococcus furiosus is one of the most thermostable organis...
In this study the structural and thermodynamic basis of the thermal stability of proteins has been s...
SummaryDespite numerous studies, understanding the structural basis of protein stability in thermoph...
The boiled enzyme was toppled as a standard enzymology control when researchers in the 1970s started...
AbstractWe found that the CutA1 protein, from Pyrococcus horikoshii (PhCutA1), has an extremely high...
Biochemical, crystallographic, and computational data support the hypothesis that electrostatic inte...
The bases of the hyperthermostability of rubredoxin from Pyrococcus furiosus (RdPf) have been probed...
Enzymes from thermophilic and, particularly, from hyperthermophilic organisms are surprisingly stabl...
Enzymes from thermophilic and, particularly, from hyperthermophilic organisms are surprisingly stabl...
Background Thermophilic proteins sustain themselves and function at higher temperatures. Despite the...
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