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Literature summary for 1.1.1.100 extracted from

  • Karmodiya, K.; Sajad, S.; Sinha, S.; Maity, K.; Suguna, K.; Surolia, N.
    Conformational stability and thermodynamic characterization of homotetrameric Plasmodium falciparum beta-ketoacyl-ACP reductase (2007), IUBMB Life, 59, 441-449.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Plasmodium falciparum
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Renatured (Commentary)

Renatured (Comment) Organism
study on guanidinium chloride-induced isothermal and thermal denaturation. Folding/unfolding is completely reversible and a two-state process. Conformational stability, i.e. DELTAGS, and the DELTACP value for the protein unfolding, are 22.68 kcal/mole and 5.83 kcal/(mole K) Plasmodium falciparum