Are coarse-grained models apt to detect protein thermal stability? The case of OPEP force field.

ABSTRACT: We present the first investigation of the kinetic and thermodynamic stability of two homologous thermophilic and mesophilic proteins based on the coarse-grained model OPEP. The object of our investigation is a pair of G-domains of relatively large size, 200 amino acids each, with an experimental stability gap of about 40 K. The OPEP force field is able to maintain stable the fold of these relatively large proteins within the hundrend-nanosecond time scale without including external constraints. This makes possible to characterize the conformational landscape of the folded protein as well as to explore the unfolding. In agreement with all-atom simulations used as a reference, we show that the conformational landscape of the thermophilic protein is characterized by a larger number of substat

SUBMITTER: Kalimeri M 

PROVIDER: S-EPMC5238951 | biostudies-literature | 2015 Jan

REPOSITORIES: biostudies-literature