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Literature summary extracted from

  • Shukla, N.; Bhatt, A.N.; Aliverti, A.; Zanetti, G.; Bhakuni, V.
    Guanidinium chloride- and urea-induced unfolding of FprA, a mycobacterium NADPH-ferredoxin reductase: stabilization of an apo-protein by GdmCl (2005), FEBS J., 272, 2216-2224.
    View publication on PubMed

Organism

EC Number Organism UniProt Comment Textmining
1.18.1.2 Mycobacterium tuberculosis
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Renatured (Commentary)

EC Number Renatured (Comment) Organism
1.18.1.2 equilibrium unfolding of enzyme by urea is a cooperative process where no stabilization of any partially folded intermediate of protein is observed. In comparison, unfolding by guanidinium chloride proceeds through intermediates that are stabilized by interaction of protein with guanidinium chloride. At a guanidinium chloride concentration of 0.8 M, stabilization of apoprotein is observed, resulting from direct binding of the guanidinium cation to protein Mycobacterium tuberculosis