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Literature summary for 5.3.99.2 extracted from

  • Iida, T.; Nishimura, S.; Mochizuki, M.; Uchiyama, S.; Ohkubo, T.; Urade, Y.; Tanaka, A.; Inui, T.
    Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase (2008), FEBS J., 275, 233-241.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus O09114
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Renatured (Commentary)

Renatured (Comment) Organism
thermal unfolding is completely reversible at pH 4.0. Differential scanning calorimetry data show no concentration dependency. Presence of an intermediate state I between the native state N and the unfolded state U. Transition temperatures of the N-I and I-U transitions are 48.2 and 60.3°C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions Mus musculus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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thermal unfolding is completely reversible at pH 4.0, with the presence of an intermediate state I between the native state N and the unfolded state U. Transition temperatures of the N-I and I-U transitions are 48.2 and 60.3°C, respectively. In the intermediate state, the main chain retains its characteristic beta-sheet structure without side.chain interactions Mus musculus