Institut de Biologie StructuraleGrenoble / France

Contact person(s) related to this article / BRUTSCHER Bernhard / FAVIER Adrien / laguri cédric / SCHANDA Paul / Simorre Jean-Pierre

Presentation of the Biomolecular NMR Spectroscopy group

Welcome to the Biomolecular NMR Spectroscopy group.


Nuclear magnetic resonance (NMR) has become an important technique for the determination of the three-dimensional structure of biological macromolecules. The ability to characterize structure and dynamics as well as interactions with physiological partners have made NMR an essential tool for understanding biological processes. The study of molecular complexes, even in the case of weak affinity, opens up powerful opportunities for the development of pharmacologically active molecules.

We are using and actively developing solution- and solid-state NMR approaches to tackle a number of challenging biological questions. In four different teams, we focus on different biomolecular applications, and different aspects of NMR methods development. Further information can be obtained by clicking on the images below, that lead to the pages of the four teams.

For any information concerning our research, you may also contact
either Paul Schanda, head of the NMR group, or the team leaders
B. Brutscher, J. Boisbouvier, P. Schanda, J.-P. Simorre


Please click on the images to get more information about the research of the NMR teams:
NMR of large Biomolecular Assemblies
Bacterial Cell Wall
Protein & RNA folding and methods development
Solid State NMR and Dynamics


Detailed insight into dynamics in a 0.5 MDa-large enzyme from solid-state NMR. Diego’s paper is out in JACS.

An advanced isotope-labeling scheme along with proton-detected magic-angle spinning NMR provides very detailed views of motions of aromatic rings, down to 100 K, and over time scales spanning 8 orders of magnitude.
Find the manuscript HERE

Integrated NMR + EM structure determination published in Nature Communications: new method, new record!

Our latest preprint is out on the integrated structure determination from NMR and EM data. We have been able to assign, essentially to completion, the 12 x 39 kDa protein assembly TET2, the largest protein for which this such a detailed analysis has been achieved. We have developed a new approach, which jointly exploits NMR and EM data and which allowed to obtain a near-atomic-resolution structure from these data.
Find the manuscript HERE

PhD position open
Structural, dynamical and functional understanding of chaperone-based import of membrane proteins into mitochondria
Please find details in the PDF file below.

Publications 2018-2019 of the NMR group



On the cover of Cell: The mechanism of chaperones transporting membrane proteins in mitochondria

The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones.
By integrating NMR with numerous other biophysical, structural and in-vivo approaches, we have provided a detailed picture of this highly dynamic chaperone complex. Details can be found HERE

The article has been hightlighted in the "Faculty of 1000"


Structural investigation of a chaperonin in action

Many fundamental cellular functions are performed by large protein assemblies. This applies in particular to protein quality control, the process by which cells ensure the recycling or correct folding of their main constituents, in order to avoid the accumulation of poorly folded proteins, aggregates or fibrils. These large machineries - chaperones, proteases and peptidases - are complex and dynamic. The studies of such biological machines present a significant challenge, due to the very size of these particles, the complexity of their biological substrates and the structural rearrangements involved. IBS researchers have implemented an approach that combines site-specific nuclear magnetic resonance observation of very large proteins, enabled by advanced isotope labeling methods, with an in situ ATP regeneration system. Using this method, they provide functional insight into the 1-MDa large hsp60 chaperonin while processing client proteins. The results, published in Sciences Advances on September 19, 2018, reveal how the functional cycle of this complex assembly is regulated. This approach opens up new perspectives for directly studying the structures and mechanisms of various biological machines in action.
Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle. Mas G, Guan J-Y, Crublet E, Colas Debled E, Moriscot C, Gans P, Schoehn G, Macek P, Schanda P, Boisbouvier J. Science Advances 2018 September 19

Master-student/PhD and Post-Doctoral Positions in the biomolecular NMR group

We welcome applications of master students, PhD students and post-doc candidates to work on different topics of the group:
• Development of innovative solution/solid-state NMR methods and isotopic labeling approaches for the study of challenging biological systems.
• Solid–state and solution-state NMR studies of biomolecular dynamics and interactions, in a number of challenging systems in which motion is an inherent feature for function.
• Protein and RNA folding, and chaperone activity studied by combination of NMR and EM approaches.
• Antibiotic resistance: Structural and functional studies of proteins involved in the synthesis of the bacterial cell wall using liquid and solid state NMR.

Please find more details in the document below:


NMR pulse sequence tools for Bruker spectrometers

The IBS pulse sequence library consists of a combination of python setup scripts and Bruker pulse sequence programs that allow for easy use and sharing of protein NMR experiments.
Currently, the IBS library contains most of the fast NMR experiments (SOFAST-HMQC, HET-SOFAST, BEST-HSQC, BEST-TROSY, HADAMAC, ...) developed during recent years at IBS. In addition, it also contains a few basic experiments (1H-13C and 1H-15N HSQC, 15N T1, T2 and HETNOE, ...), as well as tools for pulse calibration, setup of composite pulse decoupling, and advanced data processing.

The IBS library can be downloaded here


Our group is in charge of several platforms for high-field NMR spectroscopy and preparation of biological samples. Please visit the links below for more information.


Credit photo CEA/D.Morel

Our group uses state-of-the-art NMR equipment for solution- and solid-state NMR.
With 6 spectrometers from 600 MHz to 950 MHz field strength, the NMR platform at IBS is among the best-equipped sites in Europe.

The NMR platform at IBS, in partnership with the NMR platform at CRMN Lyon, is part of national and European large-scale facilities, that grant access to our high-field NMR spectrometers to external users.
IR-RMN (French large-scale NMR facility):
European NMR facility
RALF-NMR (Rhone-Alpes Large-Scale NMR facility)

We also offer a service for protein quality control (purity, oligomerization state, degree of structure). For more details, see
1D quality control platform


The production of functional protein samples with suitable isotopic labeling patterns, either by bacterial expression or cell-free synthesis, is a crucial requirement for NMR spectroscopic studies. In our dedicated wetlab facilities, we develop innovative isotope labeling schemes for solution- and solid-state NMR samples.
The expertise is also available to external users via our isotope labeling and the cell-free expression platforms.


The full list of publications can be found here