Unknown

Dataset Information

0

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.

SUBMITTER: Sterpone F 

PROVIDER: S-EPMC3775309 | biostudies-literature | 2012 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Thermophilic proteins: insight and perspective from in silico experiments.

Sterpone Fabio F   Melchionna Simone S  

Chemical Society reviews 20111005 5


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 p  ...[more]

Similar Datasets

| S-EPMC2873828 | biostudies-literature
| S-EPMC9706030 | biostudies-literature
| S-EPMC4224375 | biostudies-literature
| S-EPMC3489541 | biostudies-literature
| S-EPMC2139990 | biostudies-literature
| S-EPMC5854655 | biostudies-literature
| S-EPMC3177088 | biostudies-literature
| S-EPMC3527711 | biostudies-literature
| S-EPMC9413235 | biostudies-literature
| S-EPMC6704238 | biostudies-literature