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., Analysis of the Conformational Landscape of the N-Domains of the AAA ATPase p97: Disentangling the Continuous Conformational Variability in Partially Symmetrical Complexes. Int J Mol Sci, 2024. 25(6). https
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and international environment. The successful candidate will join Martin Blackledge's group, Protein Dynamics and Flexibility by NMR. Where to apply Website https://emploi.cnrs.fr/Offres/CDD/UMR5075
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, by integrating image analysis and docking across multiple structural states. The new tools will be validated through their application to VCP/p97 data, a key protein that plays a central role in
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. Analysis of the Conformational Landscape of the N-Domains of the AAA ATPase p97: Disentangling the Continuous Conformational Variability in Partially Symmetrical Complexes. Int J Mol Sci. 2024;25. https
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topic: This position falls within the field of bioenergetics and protein biochemistry. The project aims to study the role of an original extra-membrane structural module involved in the mechanism
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interaction with research teams in Strasbourg and Marseille. Cytochrome bd oxidases are a family of membrane proteins who catalyze the reduction of oxygen in water. They are present only in prokaryotic species
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Inria, the French national research institute for the digital sciences | Villers les Nancy, Lorraine | France | 15 days ago
macromolecular complexes (~5.5 billion frames) [1], and the first MDDB node in France ComPASS, a graph-based method for identifying communication networks in protein–protein and protein–nucleic-acid assemblies [2
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Framework Programme? Not funded by a EU programme Is the Job related to staff position within a Research Infrastructure? No Offer Description Protein pea is cultivated for the high nutritional value of its
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are important modifiable factors that influence metabolic processes and the gut microbiota. Current recommendations advocate for an adapted diet, with a reduction in animal proteins in favor of plant-based
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sequencing data at the heart of the project. From a single gene, our cells can produce different versions of a protein through a mechanism called "alternative splicing." Genetic mutations can disrupt this