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.
Research Internship "Protein purification"
PhD and Post-Doctoral Positions in the biomolecular NMR group available
We currently have several openings to work on different topics of the group:
Please find more details in the document below:
Direct insight into overall rocking motion of a protein a crystals
We recently directly observed, for the first time, how protein molecules "rock" inside protein crystals. By a unique combination of solid-state NMR spectroscopy, molecular dynamics simulations and x-ray diffraction we provided evidence that this motion is a key determinant for resolution in X-ray experiments, and also solid-state NMR.
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.
The IBS library can be downloaded here
Atomistic views of interactions in an intact bacterial cell wall
The bacterial cell wall is the primary target of antibiotic strategies. Understanding how the peptidoglycan - the major polymer forming the cell wall - is built, is therefore of crucial importance. Ironically, we know very little about the the interactions of proteins which are responsible for building the cell wall on an Spectroscopyatomic level. This relates to the fact that most structural biology techniques fail at seeing the cell wall at atomic resolution: the cell wall is large, heterogeneous and of course non-crystalline.
PLATFORMS MANAGED BY THE NMR GROUP
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.
HIGH FIELD NMR SPECTROSCOPY
Credit photo CEA/D.Morel
Our group uses state-of-the-art NMR equipment for solution- and solid-state NMR.
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.
We also offer a service for protein quality control (purity, oligomerization state, degree of structure). For more details, see
PROTEIN PRODUCTION & WET LAB EQUIPMENT
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.
Observing the overall rocking motion of a protein in a crystal.
Probing Transient Conformational States of Proteins by Solid-State R1ρ Relaxation-Dispersion NMR Spectroscopy
The RNA-binding region of human TRBP interacts with microRNA precursors through two independent domains.
Interaction of non-structural protein 5A of hepatitis C virus with SH3 domains using non-canonical binding sites.
Structure of Enterococcus faeciuml,d-Transpeptidase Acylated by Ertapenem Provides Insight into the Inactivation Mechanism.
Real-time NMR characterization of structure and dynamics in a transiently populated protein folding intermediate.
Site-resolved measurement of microsecond-to-millisecond conformational-exchange processes in proteins by solid-state NMR spectroscopy.
Plevin, M. J., D. L. Bryce, and J. Boisbouvier.
Second double-stranded RNA binding domain of dicer-like ribonuclease 1: structural and biochemical characterization.
Dynamics induced by β-lactam antibiotics in the active site of Bacillus subtilis L,D-transpeptidase.
Stereospecific isotopic labeling of methyl groups for nmr spectroscopic studies of high-molecular-weight proteins.
The full list of publications can be found here