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virus-DNP-NMR SIGNED

Development of high-field DNP-enhanced MAS NMR techniques for structure determination of viral capsids

Total Cost €

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EC-Contrib. €

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Partnership

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Project "virus-DNP-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
title: n.a.
name: n.a.
surname: n.a.
function: n.a.
email: n.a.
telephone: n.a.
fax: n.a.

 Coordinator Country France [FR]
 Project website http://www.cnrs.fr/
 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 2015
 Duration (year-month-day) from 2015-09-01   to  2017-08-31

 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

The atomic-level characterization of large viral particles is one of the greatest challenges of modern structural biology, as well as a fundamental step for the design of effective antiviral treatments. In viruses, the viral genome (double- or single-stranded RNA or DNA) is associated to multiple copies of a capsid protein, forming predominantly icosahedral or helical architectures. These complex superstructures are often studied by X-ray crystallography and electron microscopy (EM). However, only information at low resolution is usually available from EM, and extended and flexible architectures do not provide single crystals amenable to diffraction studies. Over the last years, solid-state NMR (ssNMR) has developed into a powerful structural tool for studying structure and dynamics of solid biological samples at atomic resolution and is now uniquely positioned to complement diffraction-based techniques for the characterization of large functional assemblies. However, proteins of large size or that are available in limited amounts are still inaccessible to site-specific NMR studies. Exploiting a unique equipment available in the host institution, the project aims to remove the current bottlenecks and develop improved dynamic nuclear polarization (DNP)-enhanced ssNMR methodology to push forward the limits of applicability of this technique to macromolecular assemblies, opening new avenues to ssNMR in structural biology. Innovative experimental approaches will be developed to overcome the resolution barriers that currently limit the application of high-field DNP, and new spectroscopic tools will be introduced to allow the structure determination of biomolecules under DNP conditions. The effectiveness and versatility of the newly developed methods will be tested on two viral nucleocapsids of different architectures, the icosahedral capsid of non-tailed bacteriophage AP205 and the filamentous, helical nucleocapsid of Measles virus.

 Publications

year authors and title journal last update
List of publications.
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
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 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: , ISSN: 0926-2040, DOI: 10.1016/j.ssnmr.2017.07.004
Solid State Nuclear Magnetic Resonance in press 2019-06-18

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