Séminaire du LPTMS : Alessandra Carbone (IBPS Sorbonne)


11:00 - 12:00

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The complexity of protein interactions

Alessandra Carbone (Sorbonne University, CNRS)


I will describe two facets of the interaction of proteins with other biological molecules. Firstly, I will define soft disordered (flexible, amorphous, or intrinsically disordered) regions in a protein with increasing numbers of bound interactors and analyze the correlation between disorder, interfaces and assembly. Secondly, I will address the question of reconstructing, ab initio, protein-protein interaction networks from protein language models and Neural Networks (NN) with memory from sequences with SENSE-PPI. SENSE-PPI addresses interactions between protein sequences, possibly intrinsically disordered, belonging to a model or non-model organism, or to different species such as human and viruses. 

K.Volzhenin, L.Bittner, A.Carbone, SENSE-PPI reconstructs protein-protein interactions of various complexities, within, across, and between species, with sequence-based evolutionary scale modeling and deep learning, BIORXIV/2023/558413 

B. Seoane, A. Carbone, Soft disorder modulates the assembly path of protein complexes, PLoS Computational Biology, 2022. 

B.Seoane, A.Carbone. The complexity of protein interactions unravelled from structural disorder, PLoS Computational Biology, 2021 

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