Application of Rigidity Theory to the Thermostabilization of Lipase A from Bacillus subtilis.

ABSTRACT: Protein thermostability is a crucial factor for biotechnological enzyme applications. Protein engineering studies aimed at improving thermostability have successfully applied both directed evolution and rational design. However, for rational approaches, the major challenge remains the prediction of mutation sites and optimal amino acid substitutions. Recently, we showed that such mutation sites can be identified as structural weak spots by rigidity theory-based thermal unfolding simulations of proteins. Here, we describe and validate a unique, ensemble-based, yet highly efficient strategy to predict optimal amino acid substitutions at structural weak spots for improving a protein's thermostability. For this, we exploit the fact that in the majority of cases an increased structural rigidity

SUBMITTER: Rathi PC 

PROVIDER: S-EPMC4803202 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature