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• W1967751522 endingPage "11332" @default.
• W1967751522 startingPage "11329" @default.
• W1967751522 abstract "The rubredoxin protein from the hyperthermophilic archaebacterium Pyrococcus furiosus was examined by a hydrogen exchange method. Even though the protein does not exhibit reversible thermal unfolding, one can determine its stability parameters-free energy, enthalpy, entropy, and melting temperature-and also the distribution of stability throughout the protein, by using hydrogen exchange to measure the reversible cycling of the protein between native and unfolded states that occurs even under native conditions." @default.
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• W1967751522 date "1997-10-14" @default.
• W1967751522 modified "2023-10-06" @default.
• W1967751522 title "Stability and dynamics in a hyperthermophilic protein with melting temperature close to 200°C" @default.
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• W1967751522 doi "https://doi.org/10.1073/pnas.94.21.11329" @default.
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