Conformation of the abortifacient protein pinellin: A circular dichroic study |
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Authors: | Zong Jin Tao Zhi Min Shen and Jen Tsi Yang |
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Institution: | (1) Shanghai Brain Research Institute, Academia Sinica, 200031 Shanghai, China;(2) Cardiovascular Research Institute, University of California, 94143-0130 San Francisco, California |
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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 -sheet (about 40%) with little -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 -helix, which leveled off at 0.25 mM surfactant. |
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Keywords: | Abortifacient protein pinellin circular dichroism conformation |
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