Fig. 1From: Enhanced trypsin thermostability in Pichia pastoris through truncating the flexible regionPrediction of the flexible regions of porcine trypsin. MD simulations were carried out in Gromacs package. The RMSF values of WT were collected at 300 K for a minimum of 10 ns. FlexPred predicted residue flexibility in trypsin using SVM approach. The approach of FoldUnfold used the expected average number of contacts per residue calculated from the amino acid sequence as an indicator of whether the given region is folded or unfoldedBack to article page