Abstract
The conformation of pinellin was studied by circular dichroism, which showed a minimum at 223 nm and a double maximum at 198–200 nm. The protein was rich in β-sheet (about 40%) with little α-helix, based on current CD analyses. It was stable betweenpH 4 and 10 beyond which it unfolded reversibly, but in alkaline solution, prolongly stored at, say,pH 12, it became irreversibly denatured. Thermal denaturation indicated a transition between 55° and 68°C; the solution at 80°C was partially renatured upon air-cooling back to room temperature. Addition of sodium dodecyl sulfate caused a sharp increase in α-helix, which leveled off at 0.25 mM surfactant.
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Tao, Z.J., Shen, Z.M. & Yang, J.T. Conformation of the abortifacient protein pinellin: A circular dichroic study. J Protein Chem 12, 387–391 (1993). https://doi.org/10.1007/BF01025038
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DOI: https://doi.org/10.1007/BF01025038