Institut de Biologie StructuraleGrenoble / France


Official opening of the CIBB 3D graphics room

The Official opening of a 3D graphics room took place on Friday 17 February in the Carl-Ivar Brandèn Building (CIBB).

This graphic room dedicated to master and doctoral courses in structural biology and on-site workshops offers 10 workstations operating under Debian linux with Nvidia 3D graphic displays and has the capacity to accommodate 20 students.

Located on the CIBB ground floor on EPN campus, this room has been provided by the IBS, the material has been financed by the Labex “Grenoble Alliance for Integrated Structural & Cell Biology” (GRAL) and the UFR Biology-Chemistry of University Grenoble Alpes and the installation was done by some members of the Partnership in Structural Biology (PSB).

Proton-detected solid-state NMR spectroscopy of a zinc diffusion facilitator in native nanodiscs

Membrane proteins are involved in many essential processes in living cells. However, their study is complicated by the fact that they have to be extracted from the native membrane, usually by using detergents, before they can be reinserted into model membranes, such as liposomes, bicelles or protein-bounded lipid nanodiscs. In collaboration with J. Dörr and A. Killian (Membrane Biochemistry and Biohysics, Bijvoet Center for Biomolecular Research, Utrecht, NL) we have shown that so-called native nanodiscs containing a bacterial cation diffusion facilitator (CDF) are amenable to high-resolution solid-state NMR studies. Native nanodiscs were obtained by the detergent-free extraction of the CDF protein from bacterial native membranes using Styrene Maleic Acid (SMA) copolymer. We observed favorable NMR properties that are comparable to crystalline protein preparations. This opens the way to studies of structure and dynamics of integral membrane proteins at atomic resolution in an environment that very closely resembles the native lipid bilayer.

Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs. Bersch B, Dörr JM, Hessel A, Killian JA, Schanda P. Angew Chem Int Ed Engl. 2017 Jan 27. doi: 10.1002/anie.201610441.

A new NMR tool for probing functional protein dynamics

Structural biology has produced an impressive amount of high-resolution structural information on ground-state conformations of proteins. It has long been recognized, however, that biomolecules are dynamic ensembles rather than static entities, and that alternative high-energy conformations can play important functional roles, or may be responsible for the onset of misfolding and aggregation leading to cellular deregulation and disease. NMR spectroscopy is unique in its ability to study conformational dynamics over a wide range of time scales, simultaneously for a large number of individual nuclear sites in the molecule. In particular, micro- to millisecond time-scale dynamics can be accessed by relaxation−dispersion NMR, while states involving even higher energy barriers are best studied by real-time NMR methods. In this work, we have combined these two powerful NMR techniques, enabling the detection of conformational exchange dynamics in short-lived excited protein states. Application to the major folding intermediate of the amyloidogenic protein 2-microglobulin revealed the presence of a monomer-dimer exchange process that may be responsible for the early aggregation steps leading to amyloidosis in patients under hemodialysis treatment.

Probing Conformational Exchange Dynamics in a Short-Lived Protein Folding Intermediate by Real-Time Relaxation–Dispersion NMR. FrancoSergio R, Caballero G, Ayala I, Favier A and Brutscher B. Journal of the American Chemical Society; 139(3):1065-1068