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BOLD-NMR TERMINATED

Biomolecular structures elucidated by cOLD magic angle spinning NMR with dynamic nuclear polarization

Total Cost €

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EC-Contrib. €

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Partnership

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 BOLD-NMR project word cloud

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

huntington    significantly    diseases    structural    aggregates    parkinson    ult    compatible    magic    expensive    neurodegenerative    loop    schemes    2d    isotopic    limitations    afford    labelling    hyperpolarization    samples    global    environment    tissue    multiple    dnp    characterization    demonstrated    abundance    fibrillar    brain    molecular    15n    dynamic    glutamine    uniformly    structure    closed    routinely    detecting    facilitated    spinning    native    rely    tool    polyq    combined    disease    atomic    biomolecules    solid    difficulty    commercially    he    labelled    structures    toxicity    magnetic    proteinaceous    13c    mas    notably    implicated    contacts    solution    vision    amyloid    invaluable    nmr    severe    methodology    dependent    ultra    nuclear    technique    temperature    polarization    natural    vitro    probes    alzheimer    sensitivity    distance    angle    plaque    dynamical    diffraction    fibril    resonance    levels    cryostat    poly    proved    fibrils    inter    suitable    distances    situ    mechanisms    resolution   

Project "BOLD-NMR" data sheet

The following table provides information about the project.

Coordinator
COMMISSARIAT A L ENERGIE ATOMIQUE ET AUX ENERGIES ALTERNATIVES 

Organization address
address: RUE LEBLANC 25
city: PARIS 15
postcode: 75015
website: www.cea.fr

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

 Coordinator Country France [FR]
 Project website https://sites.google.com/site/dnpgrenoble/home
 Total cost 173˙076 €
 EC max contribution 173˙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-2017
 Funding Scheme MSCA-IF-EF-ST
 Starting year 2018
 Duration (year-month-day) from 2018-04-26   to  2020-04-25

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    COMMISSARIAT A L ENERGIE ATOMIQUE ET AUX ENERGIES ALTERNATIVES FR (PARIS 15) coordinator 173˙076.00

Map

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 Project objective

Magic angle spinning solid-state nuclear magnetic resonance (MAS-NMR) has proved to be an invaluable tool in the structural and dynamical characterization at atomic resolution of biomolecules that are not suitable for solution NMR or diffraction studies, notably amyloid fibrils. These proteinaceous aggregates are implicated as the cause of many neurodegenerative diseases, such as Huntington’s, Alzheimer’s, and Parkinson’s diseases. Due to severe sensitivity limitations and the difficulty in detecting long-distance contacts in uniformly 13C/15N labelled systems, the characterization of these fibrils has been carried out in-vitro using multiple expensive samples with specific isotopic labelling schemes. In addition, it has been demonstrated that fibrils can adopt various, environment-dependent structures, which result in different levels of toxicity. The global objective of this proposal is to develop a new approach for the structural characterization at atomic resolution of biomolecules, which will be compatible in a long-term vision with native in-situ samples, as for example fibrillar plaque obtained from brain tissue. This would be invaluable in understanding the mechanisms of fibril formation in neurodegenerative diseases. The concrete approach will rely on the use of samples at natural isotopic abundance studied with an emerging hyperpolarization technique ULT-MAS-DNP (Magic Angle Spinning Dynamic Nuclear Polarization at Ultra Low Temperature). The sensitivity of the commercially available MAS-DNP technique will be significantly improved by the combined use of a unique closed-loop He cryostat (allowing ULT) with high-spinning NMR probes. This will routinely afford the sensitivity required for 13C/15N 2D NMR measurements on natural isotopic abundance samples, including the facilitated measurement of inter-molecular distances. This methodology will be applied to solve the structure of challenging poly- glutamine (polyQ) fibrils implicated in Huntington’s disease.

 Publications

year authors and title journal last update
List of publications.
2019 Adam N. Smith, Katharina Märker, Sabine Hediger, Gaël De Paëpe
Natural Isotopic Abundance 13 C and 15 N Multidimensional Solid-State NMR Enabled by Dynamic Nuclear Polarization
published pages: 4652-4662, ISSN: 1948-7185, DOI: 10.1021/acs.jpclett.8b03874
The Journal of Physical Chemistry Letters 10/16 2020-04-11
2018 Adam N. Smith, Katharina Märker, Talia Piretra, Jennifer C. Boatz, Irina Matlahov, Ravindra Kodali, Sabine Hediger, Patrick C. A. van der Wel, Gaël De Paëpe
Structural Fingerprinting of Protein Aggregates by Dynamic Nuclear Polarization-Enhanced Solid-State NMR at Natural Isotopic Abundance
published pages: 14576-14580, ISSN: 0002-7863, DOI: 10.1021/jacs.8b09002
Journal of the American Chemical Society 140/44 2020-04-11

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