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BOLD-NMR TERMINATED

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

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EC-Contrib. €

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Partnership

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 Outcomes and results

 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.

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

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.
telephone: n.a.
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

 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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