Structural Biology and Chemistry Department Seminar
Tuesday 2 April 2019 at 2.00 pm
AUDITORIUM CENTRE F. JACOB room – CFJ RdC 17c
Dr. Paolo DE LOS RIOS
Ecole Polytechnique Fédérale de Lausanne – EPFL, Faculté de Sciences de Base Institut de Physique, Laboratoire de Biophysique Statistique
Non-equilibrium protein folding (and unfolding) in the cell.
Anfinsen’s experiments in the 1960s taught us that proteins can fold by themselves, to a certain extent. These results have been correctly interpreted as a sign that the functional, natively folded state is the minimum of the free-energy landscape of proteins. Nonetheless, folding being a complex process over a rugged landscape, proteins might be trapped into metastable states for long times and, ultimately, aggregate. Furthermore, because of mutations or external stresses, the native state might not be the minimum of the free-energy, leading to spontaneous protein denaturation.
Chaperones supervise protein folding and allow proteins to fold correctly by an energy-consuming process. Here we show that, as a consequence, the native state of proteins can be preserved even under conditions that do not promote protein native folding, characterizing thus the native state as a non-equilibrium stationary state.
Contact: Alexandre Chenal
Unité de Biochimie des Interactions Macromoléculaires
INSTITUT PASTEUR – 28, rue du Docteur Roux – 75015 Paris