title: Thermophilic proteins: insight and perspective from in silico experiments.
abstract: 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.
authors: Laboratoire de Biochimie Théorique, CNRS, UPR9080, Univ Paris Diderot, Sorbonne Paris Cité, 13 rue Pierre et Marie Curie, 75005, Paris, France. fabio.sterpone@ibpc.fr
authors: Fabio
authors: F
authors: Sterpone
authors: Simone
authors: S
authors: Melchionna
mesh_terms: D020134:Catalytic Domain; D056004:Molecular Dynamics Simulation; D055550:Protein Stability; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D011789:Quantum Theory; D013696:Temperature; D013816:Thermodynamics
chemical_list: D011506:Proteins