Interface matters: the stiffness route to stability of a thermophilic tetrameric malate dehydrogenase.

ABSTRACT: In this work we investigate by computational means the behavior of two orthologous bacterial proteins, a mesophilic and a thermophilic tetrameric malate dehydrogenase (MalDH), at different temperatures. Namely, we quantify how protein mechanical rigidity at different length- and time-scales correlates to protein thermophilicity as commonly believed. In particular by using a clustering analysis strategy to explore the conformational space of the folded proteins, we show that at ambient conditions and at the molecular length-scale the thermophilic variant is indeed more rigid that the mesophilic one. This rigidification is the result of more efficient inter-domain interactions, the strength of which is further quantified via ad hoc free energy calculations. When considered isolated, the ther

SUBMITTER: Kalimeri M 

PROVIDER: S-EPMC4250060 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature