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Literature summary for 3.1.1.1 extracted from

  • DAuria, S.; Herman, P.; Lakowicz, J.; Bertoli, E.; Tanfani, F.; Rossi, M.; Manco, G.
    The thermophilic esterase from Archaeoglobus fulgidus: Structure and conformational dynamics at high temperature (2000), Proteins Struct. Funct. Genet., 38, 351-360.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Archaeoglobus fulgidus O28558
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Purification (Commentary)

Purification (Comment) Organism
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Archaeoglobus fulgidus

Synonyms

Synonyms Comment Organism
AFEST
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Archaeoglobus fulgidus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
80
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Archaeoglobus fulgidus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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between 20°C and 60°C a small but significant decrease of the beta-sheet bands occurrs, indicating a partial loss of beta-sheets. This suggests the presence of a temperature-sensitive beta-sheet. The increase in temperature from 60°C to 98°C induces a decrease of alpha-helix and beta-sheet bands which are still detected at 98°C indicating that at this temperature some secondary structure elements of the protein remain intact. The conformational dynamics of the esterase investigated by frequency-domain fluorometry and anisotropy decays show that the temperature affects the protein conformational dynamics Archaeoglobus fulgidus