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

Total Cost €


EC-Contrib. €






 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.

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

Project "BOLD-NMR" data sheet

The following table provides information about the project.


Organization address
address: RUE LEBLANC 25
city: PARIS 15
postcode: 75015

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
 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


Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 


 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.


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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