Journal
CHEMICAL SOCIETY REVIEWS
Volume 41, Issue 5, Pages 1665-1676Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1cs15199a
Keywords
-
Categories
Funding
- European Research Council [ERC-2010-StG, 258748- Thermos]
Ask authors/readers for more resources
Proteins from thermophilic and hyperthermophilic organisms are stable and function at high temperatures (50-100 degrees 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
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available