Protein Thermostability and Applications

While the adaptation of the cell inventory is important, it is a challenge for proteins to overcome high temperature in order to remain folded in the correct three-dimensional structure while maintaining adequate flexibility for their desired function. Hence, elucidation of the molecular basis of protein stability at high temperature continues to attract researcher over a broad range of disciplines. In this regards, we have used crystal structure analysis, the graph-theory approach and structure-based metrics to unveiled the structural determinants linked to protein stability of a biotechnologically important enzyme. The study revealed that augmenting N-terminal to C-terminal non-covalent interactions is associated with enhancement of the stability of the enzyme. It is proposed that mutations at the termini could be exploited to modulate protein stability in diverse folds where N- and C-termini are close together in three-dimensional space. Eventually, such studies should help in understanding the evolution and utilization of interactions between termini in the protein universe, and in developing effective protein engineering strategies.