PhD thesis (M/F) - Chemical biology of intrinsically disordered protein domains
CNRS
Research Center, Browse similar opportunities
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Research Center, Browse similar opportunities
The project will be conducted in the Biosystems Chemistry group within the interdisciplinary unit UMR 7242 Biotechnology and Cellular Signalling directed by CNRS and the University of Strasbourg and located at the Superior School of Biotechnology at the Illkirch campus. The research unit is composed of 9 research groups working on different topics such as integrity of the genome and membrane signalling. The research approaches combine functional genomics and chemical biology. The research in our team focuses on the application of chemical protein synthesis to solve complex problems in protein science. The necessary facilities for conducting the work will be provided such as chemical synthesis of peptides by solid-phase synthesis, characterization by HPLC and mass-spectrometry, as well as state-of-the-art NMR spectroscopy. Currently, our team is composed of 2 postdoctoral researchers and 3 PhD students.
We are searching for a highly motivated candidate, skilled in organic synthesis and eager to learn biological assays. Previous experience in peptide synthesis will be a strong advantage.
The candidate will integrate into the team of Biosystelms Chemistry at UMR 7242 and will be enrolled in the ED222 doctoral school in Chemistry, which requires to follow the rules of the doctoral education.
For more information, please, see web-site: https://torbeevlab.com .
The doctoral thesis work will be part of the ANR project ChemBioIDP. The goal of our research at the chemistry - biology interface is to understand the biological mechanisms involving intrinsically disordered protein regions. The proteins of interest are transcriptional coactivators ACTR (p160) and p300/CBP. These proteins are overexpressed in various cancers and participate in the formation of multiprotein complexes with nuclear receptors to regulate the transcription of multiple genes. The interaction domains - activation domain of ACTR and nuclear coactivator binding domain (NCBD) of p300/CBP - can be chemically synthesized, therefore non-canonical amino acids can be efficiently incorporated in these domains. These modifications enable optimisation of their conformational properties and improving the stability of the resulting protein complexes. The candidate with perform chemical synthesis of various analogues of protein interaction domains, including their vectorisation for delivery into cells, the study of of their effects onto nuclear receptor mediated gene transcription, as well as structural studies (by NMR, X-ray crystallography and cryo-EM).
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