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Literature summary for 3.4.22.6 extracted from

  • Lopez-Arenas, L.; Solis-Mendiola, S.; Padilla-Zuniga, J.; Hernandez-Arana, A.
    Hofmeister effects in protein unfolding kinetics: estimation of changes in surface area upon formation of the transition state (2006), Biochim. Biophys. Acta, 1764, 1260-1267.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Carica papaya
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Source Tissue

Source Tissue Comment Organism Textmining
latex
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Carica papaya
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pH Stability

pH Stability pH Stability Maximum Comment Organism
1.5
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protein unfolds following biphasic kinetics. Two different effects of electrolyte concentration on unfolding reaction are observed. At low ionic strength, the ionic atmosphere causes an increase in reaction rates, regardless of the type of ions being present. This effect is attributed to a general electrostatic screening of charge-charge interactions in the macromolecule. At high ionic strength, each electrolyte exerts a distinctly different effect: both rate constants are largely increased by guanidinium-HCl but slightly by LiCl. Na2SO4 decreases the value of both unfolding rates Carica papaya