COMPLEX-fastMAS-NMR SIGNED
Structure of a large non-crystalline multiprotein assembly by solid-state nuclear magnetic resonance with ultra-fast magic-angle spinning
Total Cost €
0EC-Contrib. €
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Project "COMPLEX-fastMAS-NMR" data sheet
The following table provides information about the project.
| Coordinator |
CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS
Organization address contact info |
| Coordinator Country | France [FR] |
| Project website | http://perso.ens-lyon.fr/guido.pintacuda |
| Total cost | 185˙076 € |
| EC max contribution | 185˙076 € (100%) |
| Programme |
1. H2020-EU.1.3.2. (Nurturing excellence by means of cross-border and cross-sector mobility) |
| Code Call | H2020-MSCA-IF-2014 |
| Funding Scheme | MSCA-IF-EF-ST |
| Starting year | 2016 |
| Duration (year-month-day) | from 2016-01-01 to 2018-01-18 |
Partnership
Take a look of project's partnership.
| # | ||||
|---|---|---|---|---|
| 1 | CENTRE NATIONAL DE LA RECHERCHE SCIENTIFIQUE CNRS | FR (PARIS) | coordinator | 185˙076.00 |
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Project objective
Extrapolating from protein structure to function is an operation difficult to accomplish, as most functions in the cell are not carried out by single proteins, but by macromolecular complexes containing multiple subunits endowed with specific functions. Despite the many advances in structural and biochemical studies of isolated molecules, a comprehensive portrait of cell biochemistry must thus include insights of the supramolecular network of interactions among the individual constituents. The structure determination of large and dynamical protein ensembles presents a great deal of challenges for X-ray diffraction techniques, and for solution nuclear magnetic resonance (NMR) due to the large size of these objects. Consequently, there is little information available today on the overall organization of the assembly subunits, their interactions, and sometimes their precise function within the cell. High-resolution solid-state NMR (ssNMR) has recently developed as a powerful structural tool for studying structure and dynamics of solid biological samples at atomic resolution. A number of issues remain however to be addressed before ssNMR is ready to cope with large-sized multi-domain functional assemblies. The proposed project aims to capitalize on new concepts recently introduced by the host institution, to implement innovative solid-state NMR methodologies. Sophisticated experimental approaches will be introduced at high magnetic field, in combination with ultra-fast magic angle spinning (MAS), enabling the structure characterization of non-crystalline assemblies that cannot be currently carried out by any other experimental technique, and notably, the determination at atomic level of the structural details that govern protein-protein interactions in functional assemblies. As a benchmark, we will tackle the interaction mode of the ring-shaped hexameric DnaB helicase with its partner DnaC, an assembly that controls the origin of the DNA replication in E. coli.
Publications
| year | authors and title | journal | last update |
|---|---|---|---|
| 2017 |
Diane Cala-De Paepe, Jan Stanek, Kristaps Jaudzems, Kaspars Tars, Loren B. Andreas, Guido Pintacuda Is protein deuteration beneficial for proton detected solid-state NMR at and above 100Â kHz magic-angle spinning? published pages: 126-136, ISSN: 0926-2040, DOI: 10.1016/j.ssnmr.2017.07.004 |
Solid State Nuclear Magnetic Resonance 87 | 2019-06-18 |
| 2016 |
Jan Stanek, Loren B. Andreas, Kristaps Jaudzems, Diane Cala, Daniela Lalli, Andrea Bertarello, Tobias Schubeis, Inara Akopjana, Svetlana Kotelovica, Kaspars Tars, Andrea Pica, Serena Leone, Delia Picone, Zhi-Qiang Xu, Nicholas E. Dixon, Denis Martinez, Mélanie Berbon, Nadia El Mammeri, Abdelmajid Noubhani, Sven Saupe, Birgit Habenstein, Antoine Loquet, Guido Pintacuda NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils published pages: 15504-15509, ISSN: 1433-7851, DOI: 10.1002/anie.201607084 |
Angewandte Chemie International Edition 55/50 | 2019-06-18 |
| 2017 |
Mukul G. Jain, Daniela Lalli, Jan Stanek, Chandrakala Gowda, Satya Prakash, Tom S. Schwarzer, Tobias Schubeis, Kathrin Castiglione, Loren B. Andreas, P. K. Madhu, Guido Pintacuda, Vipin Agarwal Selective 1 H– 1 H Distance Restraints in Fully Protonated Proteins by Very Fast Magic-Angle Spinning Solid-State NMR published pages: 2399-2405, ISSN: 1948-7185, DOI: 10.1021/acs.jpclett.7b00983 |
The Journal of Physical Chemistry Letters 8/11 | 2019-06-18 |
| 2016 |
Loren B. Andreas, Kristaps Jaudzems, Jan Stanek, Daniela Lalli, Andrea Bertarello, Tanguy Le Marchand, Diane Cala-De Paepe, Svetlana Kotelovica, Inara Akopjana, Benno Knott, Sebastian Wegner, Frank Engelke, Anne Lesage, Lyndon Emsley, Kaspars Tars, Torsten Herrmann, Guido Pintacuda Structure of fully protonated proteins by proton-detected magic-angle spinning NMR published pages: 9187-9192, ISSN: 0027-8424, DOI: 10.1073/pnas.1602248113 |
Proceedings of the National Academy of Sciences 113/33 | 2019-06-18 |
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