Changes in soybean trypsin inhibitor by varying pressure and temperature of processing: A molecular modeling study

摘要

In recent years, molecular dynamic (MD) simulations have been used to understand the effects of various processing methods on the structural properties and stability of proteins. In this study, the conformational changes in soybean trypsin inhibitor molecule were evaluated with the use of high temperature and pressure. The MD simulations have been performed at various temperatures (300 K, 345 K and 373 K) and pressure (1 bar, 3 kbar, 6 kbar) combinations. The results showed that the soybean trypsin inhibitor (STI) molecule is relatively stable at high temperatures, primarily due to the presence of disulphide bonds. However, at higher pressures, significant compaction was observed. Root mean square deviations, Radius of gyration and volume of the STI molecule were evaluated. Furthermore, Ramachandran plots were used to evaluate the stability of the various simulated molecules. It was found that the compaction resulted in high steric interferences among the core residues.