Dr. Mehdi D. Davari Department of Bioorganic Chemistry, Leibniz Institute of Plant Biochemistry, Weinberg 3,06120 Halle, Germany, Email: mehdi.davari@ipb-halle.de Abstract. The ability to tailor protein function underpins progress in biotechnology, medicine, and sustainable biocatalytic processes. Yet the immense size of protein sequence space, combined with experimental limitations in screening capacity,…
Francois Dehez LPCT, CNRS, Université de Lorraine, Nancy
Charles L. Brooks IIICyrus Levinthal Distinguished University Professor of Chemistry and BiophysicsWarner-Lambert/Parke-Davis Professor of ChemistryProfessor of Chemistry and Professor of BiophysicsChair of BiophysicsDepartments of Chemistry and BiophysicsUniversity of Michigan Abstract.Exploiting sequence to function relationships is fundamental to the methodology of directed evolution in the context of biocatalyst discovery and design.…
A. Sofia F. OliveiraUniversity of Bristol, Bristol, BS81TS, UKEmail: sofia.oliveira@bristol.ac.uk Abstract. Proteins are neither static entities nor work in isolation under physiological conditions. In fact, it is the opposite; their function is closely linked to their ability to adopt and transition between multiple conformational states, with even subtle environmental changes…
Frederic Cazals Frederic.Cazals@inria.frCentre Inria d’Université Côte d’Azur, Algorithms-Biology-Structure Abstract The function of proteins relies on a subtle mix between structural and dynamical properties (thermodynamics, kinetics). Deep learning based methods, pioneered by AlphaFold, for which the 2024 Nobel prize in chemistry was co-awarded, have revolutionized protein structure prediction and enabled the…
Luiz Felipe Piochi1, Di Tang2, Johan Malmström2, Yasaman Karami1, Hamed Khakzad1,* 1 Université de Lorraine, CNRS, Inria, LORIA, F-54000 Nancy, France2 Division of Infection Medicine, Department of Clinical Sciences Lund, Faculty of Medicine,Lund University, Lund, Sweden AbstractProtein-protein interaction (PPI) prediction remains sparse for bacteria and host-pathogen systems, limiting mechanistic insight…
We are happy to announce that the second NCSB will be held on June 19th, 2025 at Nancy , with the support of the Centre Inria de l’Universite de Lorraine, LORIA and GDR BIMMM. We have the pleasure of hosting internationally distinguished experts in computational and structural biology. Here is…
Omid Mokhtari Inria, Loria, CNRS, Universite de Lorraine, Nancy Proteins are dynamic entities, and their conformational flexibility, particularly in intrinsically disordered regions (IDRs), plays a crucial role in their function. While significant progress has been made in predicting protein-protein interfaces, existing methods often overlook conformational heterogeneity. We employ state-of-the-art geometric…
Martin Pacesa LPDI, EPFL, Switzerland Protein–protein interactions (PPIs) are at the core of all key biological processes. However, the complexity of the structural features that determine PPIs makes their design challenging. We present BindCraft, an open-source and automated pipeline for de novo protein binder design with experimental success rates of…
BIGNON Emmanuelle;A QIU Yuya;A SMIRNOVA Ekaterina;B SCHULTZ Patrick;B PAPAI Gabor;B BEN SHEM AdamB A) Université de Lorraine and CNRS, UMR 7019 LPCT, Nancy, France; B) Department of Integrated Structural Biology, IGBMC, CNRS and INSERM, UMR 7104-UMR-S 1258, Illkirch, France emmanuelle.bignon@univ-lorraine.fr Gene activity is tightly controlled by reversible chemical modifications called…