How conformational flexibility stabilizes the hyperthermophilic elongation factor G-domain.

ABSTRACT: Proteins from thermophilic organisms are stable and functional well above ambient temperature. Understanding the molecular mechanism underlying such a resistance is of crucial interest for many technological applications. For some time, thermal stability has been assumed to correlate with high mechanical rigidity of the protein matrix. In this work we address this common belief by carefully studying a pair of homologous G-domain proteins, with their melting temperatures differing by 40 K. To probe the thermal-stability content of the two proteins we use extensive simulations covering the microsecond time range and employ several different indicators to assess the salient features of the conformational landscape and the role of internal fluctuations at ambient condition. At the atomistic le

SUBMITTER: Kalimeri M 

PROVIDER: S-EPMC4241466 | biostudies-literature | 2013 Nov

REPOSITORIES: biostudies-literature