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]

 


Proposition de thèse susceptible d'être financé (financement Paris Diderot, ED 388).

Analyse structurale et dynamique des protéines régulatrices de l’expression du génome chloroplastique et de leurs interactions avec les ARN messagers

Potential candidates should send a letter of motivation, CV, and a recent M1 (and M2 if available) grades report to robert at ibpc dot fr by 13 June 2018.


 

Structure, dynamics and interactions of biological macromolecules

Research

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, predicting — or even understanding— 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 by combining a few recurring elements: physical-chemical reasoning, mathematical analysis, and computer simulation?

Selected examples

Collaborations

Frédéric Cazals   Pinak Chakrabarti   Joël Janin   David Perahia

Recent publications

2017
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.

[see all publications]