Literature summary extracted from

Powers, S.L.; Robinson, C.R.; Robinson, A.S.
Denaturation of an extremely stable hyperthermophilic protein occurs via a dimeric intermediate (2007), Extremophiles, 11, 179-189.

Organism

EC Number	Organism	UniProt	Comment	Textmining
3.2.1.B28	Pyrococcus furiosus	Q51723	-	-

Temperature Stability [°C]

EC Number	Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
3.2.1.B28	90	-	protein unfolds at 90°C with an overall DELTAG° of about 20 kcal/mol. Unfolding proceeds via a three-state pathway that includes a stable intermediate species. Stability of the native and intermediate forms is concentration dependen. A model for the denaturation of beta-glucosidase predicts that the tetramer dissociates to partially folded dimers, followed by the coupled dissociation and denaturation of the dimers to unfolded monomers	Pyrococcus furiosus

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Release 2023.1 (January 2023)