Institut de Biologie StructuraleGrenoble / France

Contact person(s) related to this article / 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 Jérôme Boisbouvier, 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


PhD and Post-Doctoral Positions in the biomolecular NMR group available

We currently have several openings 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:

Detailed insight into the motions of proteins in crystals

Room-temperature X-ray crystallography is a powerful emerging method which, in addition to providing protein structures, can also shed light onto protein dynamics. However, whether the motions in crystals are relevant biologically, or whether the packing within the crystal impacts the flexibility of proteins has been so far poorly understood.
In our recent study we have illuminated this question, by measuring directly the motions of proteins in different crystals by solid-state NMR, and comparing to microsecond-long MD simulations. Our data show that indeed the subtle balance of inter- and intra-molecular contacts has an impact can alter motions greatly, and may or may not sustain local as well as overall dynamics.

Decrypting a cellular guidance system to fight against pneumococcal infections

Accurate placement of the bacterial division site is a prerequisite for the generation of two viable and identical daughter cells. In Streptococcus pneumoniae (pneumococcus), the positive regulatory mechanism involving the membrane protein MapZ positions precisely the conserved cell division protein FtsZ at the cell centre. Reasearchers of the Institut de Biologie et de Chimie des Protéines in Lyon et of the NMR group of the IBS characterized the structure of the extracellular domain of MapZ. This structure–function analysis of MapZ, published in Nature Communications, provides the first molecular characterization of a positive regulatory process of bacterial cell division which may be helpfull to develop new antibiotics.

Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ. Sylvie Manuse, Nicolas L. Jean, Mégane Guinot, Jean-Pierre Lavergne, Cédric Laguri, Catherine M. Bougault, Michael S. VanNieuwenhze, Christophe Grangeasse & Jean-Pierre Simorre. Nature Communications, doi:10.1038/ncomms12071, Published 27 June 2016
See paper in Nature communications link


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.

Recent publications

Slow conformational exchange and overall rocking motion in ubiquitin protein crystals
V. Kurauskas, S. A. Izmailov, O. N. Rogacheva, A. Hessel, I. Ayala, J. Woodhouse, A. Shilova, Y. Xue, et al and P. Schanda,
Nat. Commun. 2017, 8, 145

Unraveling self-assembly pathways of the 468-kDa proteolytic machine TET2.
Macek P, Kerfah R, Erba EB, Crublet E, Moriscot C, Schoehn G, Amero C, Boisbouvier J.
Sci Adv. 2017 Apr 7;3(4):e1601601. doi: 10.1126/sciadv.1601601.

Structure–function analysis of the extracellular domain of the pneumococcal cell division site positioning protein MapZ.
Sylvie Manuse, Nicolas L. Jean, Mégane Guinot, Jean-Pierre Lavergne, Cédric Laguri, Catherine M. Bougault, Michael S. VanNieuwenhze, Christophe Grangeasse & Jean-Pierre Simorre. Nature Communications, doi:10.1038/ncomms12071, Published 27 June 2016 link

Studying dynamics by magic-angle spinning solid-state NMR spectroscopy: Principles and applications to biomolecules
Paul Schanda, Matthias Ernst
Progress in Nuclear Magnetic Resonance Spectroscopy, Volume 96, August 2016, Pages 1-46

Sensitive proton-detected solid-state NMR spectroscopy of large proteins with selective CH3 labelling: application to the 50S ribosome subunit
Vilius Kurauskas, Elodie Crublet, Pavel Macek, Rime Kerfah, Diego F. Gauto, Jérôme Boisbouvier Paul Schanda
Chem. Commun., 2016,52, 9558-9561

Observing the overall rocking motion of a protein in a crystal.
Peixiang Ma, Yi Xue, Nicolas Coquelle, Jens D Haller, Tairan Yuwen, Isabel Ayala, Oleg Mikhailovskii, Dieter Willbold, Jacques-Philippe Colletier, Nikolai R Skrynnikov, and Paul Schanda
Nature Communications 2015, 6: 8361-66 link

The full list of publications can be found here