HABENSTEIN, Birgit; LOQUET, Antoine

doi:10.1016/j.bpc.2015.07.003

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HABENSTEIN, Birgit

LOQUET, Antoine

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Biophysical Chemistry. 2016, vol. 210, p. 14-26

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Protein self-assemblies are ubiquitous biological systems involved in many cellular processes, ranging from bacterial and viral infection to the propagation of neurodegenerative disorders. Studying the atomic three-dimensional structures of protein self-assemblies is a particularly demanding task, as these systems are usually insoluble, non-crystalline and of large size. Solid-state NMR (ssNMR) is an emerging method that can provide atomic-level structural data on intact macromolecular assemblies. We here present recent progress in magic angle spinning ssNMR to study protein assemblies and give an overview on its combination with complementary techniques such as cryo-EM, mass-per-length measurements, SAXS and X-ray diffraction. Applications of ssNMR on its own and in hybrid approaches have revealed precious atomic details and first high-resolution structures of complex biological assemblies, including amyloid fibrils, bacterial filaments, phages or virus capsids. (C) 2015 Elsevier B.V. All rights reserved.< Réduire

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Solid-state NMR: An emerging technique in structural biology of self-assemblies

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