Tracking the corresponding state principle

Maria KALIMERI just graduated from Univ Paris VII. Congratulations! Her thesis focused on mechanical properties of thermophilic proteins explored via an innovative framework based on network analysis. Here a bite of her work "Understanding the relation between protein flexibility, stability and function remains one of the most challenging, open questions in biophysical chemistry. For example, proteins need to be flexible to facilitate substrate binding but locally rigid to sustain substrate specificity. Exemplary cases are enzymes from microorganisms that thrive at elevated temperatures, also referred to as thermophiles. These proteins are stable and functional at the high temperature regime but generally lack activity at ambient conditions. Therefore, their thermal stability has been correlated to enhanced mechanical rigidity through the corresponding states paradigm. The generality of this view, however, has been questioned by a number of

experimental and computational studies. In the present study, we employ the gold standard of computational techniques, namely Molecular Dynamics simulations, in order to identify microscopical characteristics that distinguish thermophilic from mesophilic proteins, elaborating in particular on the rigidity paradigm mentioned above." For a more complete reading see here.