Charles H. Robert


Laboratoire de Biochimie Théorique
Institut de Biologie Physico Chimique
13, rue Pierre et Marie Curie
75005 Paris


Tél: (33) [0]1 58 41 51 61
(outside France) [in France]

Structure, dynamics and interactions of biological macromolecules


Because of the intrinsic flexibility of the polypeptide or polynucleotide chain, a protein or a nucleic acid can take on an enormous number of conformations. Whether folding to attain a native form in an auto-structuration process at one extreme, or unceasingly interconverting between alternative unstructured conformations at the other, these macromolecules’ conformational dynamics, and their interactions with each other and the different components of an organism, lie at the heart of Biology.

That, in a nutshell, is one major motivation of this work: understanding Biology, with obvious practical consequences for understanding human health and pathologies, and for coming up with new therapies.

Yet because of the high dimensionality of these conformational spaces, understanding — let alone predicting— the biochemical function of a given macromolecule can be a decidedly non-trivial task. So another motivation is the challenge: how to gain insight into these intricately complex biological systems? Here this is attempted by making use of a few recurring components: physical-chemical reasoning, mathematical analysis, and computer simulation.

Selected examples


Frédéric Cazals   Pinak Chakrabarti   Joël Janin   David Perahia   Ingrid Lafontaine

Recent publications

Laurin Y, Eyer J, Robert CH, Prévost C, Sacquin-Mora S..  2017.  Mobility and core-protein binding patterns of disordered C-terminal tails in β-tubulin isotypes.. Biochemistry. 56(12):1746–1756.