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Institut de Biologie StructuraleGrenoble / France

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Solid-state NMR and dynamics team. Team leader Paul Schanda.

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Our research focus: Understanding the motion of proteins at atomic resolution and the link to molecular function

Understanding protein function at atomic level requires the characterization of protein structure, dynamics and interaction at atomic resolution. While the knowledge of the three-dimensional structures of biomolecules is an important step towards this understanding, many interesting biomolecular processes require that biomolecules dynamically explore a range of different conformational states.

Our main research interest is the characterization of proteins that rely on motion to perform their function. In particular, we are interested in understanding the mechanisms by which membrane proteins transport metabolites through the phospholipid bilayer, and furthermore the modes of action of chaperones interacting with aggregation-prone molecules. We use Nuclear Magnetic Resonance spectroscopy, both in the solid-state and in solution-state to probe structure interactions and dynamics in these systems. In parallel and complementary to these studies of biomolecular function, we actively develop and improve NMR techniques, in particular solid-state NMR approaches, which provide insight into biomolecular dynamics at increasing level of detail.
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Latest news

Native nanodiscs as a tool for membrane protein studies


Atomic-resolution studies of membrane proteins generally suffer from the need to extract the protein from its native lipid environment, which can introduce perturbations of structure and dynamics. We show that the use of a polymer allows to extract directly a patch of native membrane with the protein embedded, and this type of native nanodiscs enable high-resolution solid-state NMR studies, opening possibilities for probing structure, interactions and dynamics of membrane proteins in a near-native environment.
Find out more: Bersch et al, "Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs"

Sensitive solid-state NMR of large proteins through methyl labeling


Studying very large protein complexes is enabled by selective methyl labeling. We recently showed that CH3 labeling provides highly sensitive spectra of protein assemblies from several hundred kilodaltons to a megadalton.
Read paper Kurauskas et al, "Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit"

Direct observation of the overall rocking motion of a protein in a crystal

A combination of advanced solid-state NMR methods, X-ray crystallography and microsecond-long MD simulations has allowed to demonstrate for the first time the motion of a protein molecule inside a crystal. This motion, occurring on a microsecond time scale, is an important determinant for resolution in X-ray diffraction and solid-state NMR experiments.

Read more at Nature Communications

Key words: Protein dynamics and mechanisms * Macromolecular machines * Methods development
Mots clés: Dynamique des protéines et mécanismes * Nanomachines macromoléculaires * Développements méthodologiques