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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 €

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EC-Contrib. €

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Partnership

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 COMPLEX-fastMAS-NMR project word cloud

Explore the words cloud of the COMPLEX-fastMAS-NMR project. It provides you a very rough idea of what is the project "COMPLEX-fastMAS-NMR" about.

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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
address: RUE MICHEL ANGE 3
city: PARIS
postcode: 75794
website: www.cnrs.fr

contact info
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name: n.a.
surname: n.a.
function: n.a.
email: n.a.
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 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.

# participants  country  role  EC contrib. [€] 
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
List of publications.
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 100 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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