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Literature summary for 3.1.26.5 extracted from

  • Henkels, C.H.; Oas, T.G.
    Thermodynamic characterization of the osmolyte- and ligand-folded states of Bacillus subtilis ribonuclease P protein (2005), Biochemistry, 44, 13014-13026.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Bacillus subtilis P25814
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Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
additional information
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circular dichroism thermal denaturation studies of P protein (noncatalytic component of ribonuclease P) in the presence of stabilizing solute (osmolyte or ligand) to obtain a thermodynamic description of temperature-induced unfolding of the ligand-folded and trimethylamine N-oxide-folded conformations of P protein Bacillus subtilis