Emmanuelle Bignon
I am Emmanuelle Bignon, Postdoctoral researcher at the CBL. After obtaining my Master degree in chemistry (focused on Macromolecules, Aroma, Perfumes and Environment) at the University of Nice-Sophia Antipolis (France), I made a PhD in computational chemistry in collaboration with the Ecole Normale Supérieure and the Analytical Sciences Institute in Lyon, France. My project dealt with the understanding of the formation of DNA lesions, as well as their impact on the DNA structure, which drives their recognition by repair enzymes. Through this experience supervised by Pr. Christophe Morell and Pr. Elise Dumont, I developed strong skills in all-atom molecular dynamics simulations, quantum chemistry, and hybrid QM/MM calculations. Moreover, I acquired a strong background on biosystems and an open-mind thanks to the intense cross-talk that we maintained with experimentalist and theoretician collaborators, especially Dr. Ravanat and Dr. Douki, our biochemist collaborators working in the Acid Nucleic Laboratory of the CEA of Grenoble.
My project here at the CBL is about the S-nitrosylation (SNO), a cysteine post-translational modification that plays an important role in the redox regulation of proteins. We are working on two main points that will provide an in-depth comprehension of such an essential cellular phenomenon.
On the one hand, we are investigating the structural impact of the SNO on biologically relevant proteins, such as TRAP1 and FAK1. Indeed, S-nitrosylation of these latter may be strongly implicated in the development of human hepatocellular carcinoma. Therefore, it is important to study the structural and dynamical features of such proteins upon SNO to understand how this modification impacts their functions. For this purpose, we use classical molecular dynamics simulations but also enhanced methods such as metadynamics. Besides, we assess the force field parameters (AMBER, GROMOS and CHARMM) of the modified cysteine, in order to have a robust benchmark that will serve as framework for simulations on other S-nitrosylated systems.
On the other hand, QM calculations are performed to unravel the cysteine reactivity. We first investigate this reaction in small models with QM methods, and we aim to study them directly in relevant proteins to evaluate the impact of the amino acids surrounding by means of hybrid QM/MM calculations.
This work involves strong collaborations with experimentalists, notably with Dr. Giuseppe Filomeni from the Unit of Cell and Survival of the DCRC.
Publications: 10
Citations: 48
h-index: 5