Abstract
AbstractDisulfide bond formation is the decisive event in the protein folding to determine the conformation and stability of protein. To achieve this disulfide bond formation in vitro, we took 2,5-dimercapto-1,3,4-thiadiazole (DMcT) as a model compound. We found that disulfide bond formation takes place between two sulfhydryl groups of DMcT molecules in methanol. UV-Vis, FT-IR and mass spectroscopic as well as cyclic voltammetry were used to monitor the course of reaction. We proposed a mechanism for the solvent induced disulfide bond formation on the basis of the results we obtained.
Highlights
We have observed a colour change for the methanolic solution of DMcT from pale yellow to intense yellow within three hours
The pH of the fresh methanolic solution of DMcT is 2.1 and the pH of the solution increases as the time increases and attained a constant value of 6.8 after 48h
After 48h, the solution did not show any peak at 260 nm due to the transition involving charge transfer hydrogen bonded (CTHB) type complex in addition to enormous decrease in intensity of peak at 340 nm indicating that DMcT molecules were converted into some products which were settled as a pale yellow solid in the solution
Summary
We have observed a colour change for the methanolic solution of DMcT from pale yellow to intense yellow within three hours. The fresh methanolic solution of DMcT shows predominant peaks at 260 nm and 340 nm due to electronic transitions involving charge transfer hydrogen bonded (CTHB) type complex[5] and n→ π* transition,[6] respectively. After 48h, the solution did not show any peak at 260 nm due to the transition involving CTHB type complex in addition to enormous decrease in intensity of peak at 340 nm indicating that DMcT molecules were converted into some products which were settled as a pale yellow solid in the solution.
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