Publications by authors named "F Poitevin"

Molecules are essential building blocks of life and their different conformations (i.e., shapes) crucially determine the functional role that they play in living organisms.

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Proteins and other biomolecules form dynamic macromolecular machines that are tightly orchestrated to move, bind, and perform chemistry. Cryo-electron microscopy (cryo-EM) can access the intrinsic heterogeneity of these complexes and is therefore a key tool for understanding mechanism and function. However, 3D reconstruction of the resulting imaging data presents a challenging computational problem, especially without any starting information, a setting termed ab initio reconstruction.

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Molecules are essential building blocks of life and their different conformations (i.e., shapes) crucially determine the functional role that they play in living organisms.

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Serial femtosecond X-ray crystallography has emerged as a powerful method for investigating biomolecular structure and dynamics. With the new generation of X-ray free-electron lasers, which generate ultrabright X-ray pulses at megahertz repetition rates, we can now rapidly probe ultrafast conformational changes and charge movement in biomolecules. Over the last year, another innovation has been the deployment of Frontier, the world's first exascale supercomputer.

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Article Synopsis
  • Enzymes like isocyanide hydratase (ICH) have complex structures that make it hard to study how they catalyze reactions, but researchers used advanced techniques to observe these processes in real-time.* -
  • The active site of ICH has various shapes, and during the reaction, the formation of specific intermediates helps stabilize the configurations necessary for catalysis.* -
  • The study shows that the ionization of a specific amino acid (aspartate) during the reaction triggers structural changes in the enzyme, influencing how it functions—this reveals how electrostatic interactions control enzyme behavior.*
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