Conformation of the abortifacient protein pinellin: A circular dichroic study

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 beta-sheet (about 40%) with little alpha-helix, based on current CD analyses. It was stable between pH4 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 degrees and 68 degrees C; the solution at 80 degrees C was partially renatured upon air-cooling back to room temperature. Addition of sodium dodecyl sulfate caused a sharp increase in alpha-helix, which leveled off at 0.25 mM surfactant.

Modeling and Simulation of an Integrated Micro Packed Bed Reactor-Heat Exchanger Configuration for Direct Dimethyl Ether Synthesis

“…Extensive studies on methanol dehydration over c-Al 2 O 3 have been performed to obtain the reaction mechanism [39,45]. A similar mechanism was proposed by different research groups for HZSM-5 [48,49]. This mechanism is based on ether formation via a surface reaction between the adsorbed alcohol molecule on an acidic site and an adsorbed alkoxide anion on a basic site.…”