Proteins from thermophilic and hyperthermophilic organisms are stable and function at high temperatures (50-100 °C). The importance of understanding the microscopic mechanisms underlying this thermal resistance is twofold: it is key for acquiring general clues on how proteins maintain their fold stable and for targeting those medical and industrial applications that aim at designing enzymes that can work under harsh conditions. In this tutorial review we first provide the general background of protein thermostability by specifically focusing on the structural and thermodynamic peculiarities; next, we discuss how computational studies based on Molecular Dynamics simulations can broaden and refine our knowledge on such special class of proteins.
This journal is © The Royal Society of Chemistry 2012