Opendata, web and dolomites

FASTER SIGNED

Faster magic-angle spinning leads to a resolution revolution in biological solid-state NMR

Total Cost €

0

EC-Contrib. €

0

Partnership

0

Views

0

 FASTER project word cloud

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

structures    magnitude    breakthrough    rotation    uncharacterized    urgent    presently    detected    approx    few    proton    13c    frequencies    attainable    disease    quality    characterization    precision    medical    resolution    investigation    interaction    42    almost    enhanced    man    view    ones    solving    amount    peptide    orders    compare    revolution    determined    spinning    osaka    larger    gain    biological    experiments    beta    improvement    nmr    accessible    mas    removes    bottleneck    1h    previously    dipolar    gyromagnetic    faster    mu    proteins    employing    membrane    poor    mg    sensitive    mentioned    horizons    frontiers    200    mutant    spectroscopy    khz    spectra    sensitivity    amyloid    frequency    alzheimer    protonated    structural    caused    250    atomic    favorably    linked    amyloids    biology    questions    solid    fast    preparation    elude    object    angle    made    thanks    spectral    ratio    found    structure    solution    magic   

Project "FASTER" data sheet

The following table provides information about the project.

Coordinator
EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZUERICH 

Organization address
address: Raemistrasse 101
city: ZUERICH
postcode: 8092
website: https://www.ethz.ch/de.html

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 Switzerland [CH]
 Total cost 2˙173˙375 €
 EC max contribution 2˙173˙375 € (100%)
 Programme 1. H2020-EU.1.1. (EXCELLENT SCIENCE - European Research Council (ERC))
 Code Call ERC-2016-ADG
 Funding Scheme ERC-ADG
 Starting year 2017
 Duration (year-month-day) from 2017-10-01   to  2022-09-30

 Partnership

Take a look of project's partnership.

# participants  country  role  EC contrib. [€] 
1    EIDGENOESSISCHE TECHNISCHE HOCHSCHULE ZUERICH CH (ZUERICH) coordinator 2˙173˙375.00

Map

 Project objective

Solid-state NMR has recently made a significant impact on structural biology by providing atomic-resolution structures of several, previously uncharacterized proteins. A particularly relevant example is the Amyloid-beta (Aβ) peptide linked to Alzheimer’s disease where we determined the atomic-resolution structure of Aβ(1-42) and of the Osaka mutant of Aβ(1-40). A spectral resolution revolution is now in reach that will enable solid-state NMR to address new frontiers in structural biology. The applications mentioned above are based on 13C-detected spectroscopy. Proton-detected experiments, although clearly more sensitive thanks to the high gyromagnetic ratio of 1H, have found few applications so far, due to the poor resolution of 1H spectra caused by the 1H-1H dipolar interaction. The proton resolution can be enhanced by employing faster rotation of the sample, i.e. higher MAS (magic-angle spinning) frequencies. Presently accessible MAS frequencies are already faster than the ones of any other man-made object. A significant improvement is still attainable in our view. Increasing the MAS frequency to 200-250 kHz will improve the spectral quality to favorably compare with solution NMR for larger proteins, including fully protonated systems. In addition, the amount of sample required is reduced by almost two orders of magnitude, to approx. 100 μg, compared to the about 10 mg needed in 13C-detected experiments. This removes an important bottleneck in sample-preparation. The resolution and sensitivity gain will allow the structural characterization of e.g. disease-relevant amyloids or membrane proteins with higher precision. Moreover, this approach will enable the investigation of complex systems, which presently elude structural characterization. The resolution revolution brought about by fast spinning shall thus represent a breakthrough since it will open new horizons for solving urgent biological and medical questions.

 Publications

year authors and title journal last update
List of publications.
2019 Albert A. Smith, Matthias Ernst, Sereina Riniker, Beat H. Meier
Localized and Collective Motions in HET‐s(218‐289) Fibrils from Combined NMR Relaxation and MD Simulation
published pages: 9383-9388, ISSN: 1433-7851, DOI: 10.1002/anie.201901929
Angewandte Chemie International Edition 58/28 2020-04-24
2019 Lauriane Lecoq, Maarten Schledorn, Shishan Wang, Susanne Smith-Penzel, Alexander A. Malär, Morgane Callon, Michael Nassal, Beat H. Meier, Anja Böckmann
100 kHz MAS Proton-Detected NMR Spectroscopy of Hepatitis B Virus Capsids
published pages: , ISSN: 2296-889X, DOI: 10.3389/fmolb.2019.00058
Frontiers in Molecular Biosciences 6 2020-04-24
2019 Susanne Penzel, Andres Oss, Mai-Liis Org, Ago Samoson, Anja Böckmann, Matthias Ernst, Beat H. Meier
Spinning faster: protein NMR at MAS frequencies up to 126 kHz
published pages: 19-29, ISSN: 0925-2738, DOI: 10.1007/s10858-018-0219-9
Journal of Biomolecular NMR 73/1-2 2019-06-11
2018 Daniel Stöppler, Alex Macpherson, Susanne Smith-Penzel, Nicolas Basse, Fabien Lecomte, Hervé Deboves, Richard D. Taylor, Tim Norman, John Porter, Lorna C. Waters, Marta Westwood, Ben Cossins, Katharine Cain, James White, Robert Griffin, Christine Prosser, Sebastian Kelm, Amy H. Sullivan, David Fox, Mark D. Carr, Alistair Henry, Richard Taylor, Beat H. Meier, Hartmut Oschkinat, Alastair D. Lawson
Insight into small molecule binding to the neonatal Fc receptor by X-ray crystallography and 100 kHz magic-angle-spinning NMR
published pages: e2006192, ISSN: 1545-7885, DOI: 10.1371/journal.pbio.2006192
PLOS Biology 16/5 2019-04-26
2018 Albert A. Smith, Matthias Ernst, Beat H. Meier
Optimized “detectors” for dynamics analysis in solid-state NMR
published pages: 45104, ISSN: 0021-9606, DOI: 10.1063/1.5013316
The Journal of Chemical Physics 148/4 2019-04-26
2019 Thomas Wiegand, Riccardo Cadalbert, Denis Lacabanne, Joanna Timmins, Laurent Terradot, Anja Böckmann, Beat H. Meier
The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase
published pages: 31, ISSN: 2041-1723, DOI: 10.1038/s41467-018-07968-3
Nature Communications 10/1 2019-04-26

Are you the coordinator (or a participant) of this project? Plaese send me more information about the "FASTER" project.

For instance: the website url (it has not provided by EU-opendata yet), the logo, a more detailed description of the project (in plain text as a rtf file or a word file), some pictures (as picture files, not embedded into any word file), twitter account, linkedin page, etc.

Send me an  email (fabio@fabiodisconzi.com) and I put them in your project's page as son as possible.

Thanks. And then put a link of this page into your project's website.

The information about "FASTER" are provided by the European Opendata Portal: CORDIS opendata.

More projects from the same programme (H2020-EU.1.1.)

KineTic (2020)

New Reagents for Quantifying the Routing and Kinetics of T-cell Activation

Read More  

E-DURA (2018)

Commercialization of novel soft neural interfaces

Read More  

NEUTRAMENTH (2018)

A redox-neutral process for the cost-efficient and environmentally friendly production of Menthol

Read More