Faculty of Science, Department of Chemical Physics and Institute of Biotechnology, University of Granada, 18071-Granada, Spain. sanchezr@goliat.ugr.es
Abstract
The ability to engineer proteins with increased thermostability will profoundly broaden their practical applications. Recent experimental results show that optimization of charge-charge interactions on the surface of proteins can be a useful strategy in the design of thermostable enzymes. Results also indicate a possibility that such optimized interactions provide structural determinants for enhanced stability of proteins from thermophilic organisms. In this article, the general strategy for design of thermostable proteins and perspectives for future studies are discussed.