Sensitivity-enhanced three-dimensional and carbon-detected two-dimensional NMR of proteins using hyperpolarized water.

3D NMR BEST-HNCO Direct 13C detection Dissolution-dynamic nuclear polarization (D-DNP) Hyperpolarization Non-uniform sampling

Journal

Journal of biomolecular NMR
ISSN: 1573-5001
Titre abrégé: J Biomol NMR
Pays: Netherlands
ID NLM: 9110829

Informations de publication

Date de publication:
Mar 2020
Historique:
received: 09 09 2019
accepted: 27 01 2020
pubmed: 11 2 2020
medline: 9 10 2020
entrez: 11 2 2020
Statut: ppublish

Résumé

Signal enhancements of up to two orders of magnitude in protein NMR can be achieved by employing HDO as a vector to introduce hyperpolarization into folded or intrinsically disordered proteins. In this approach, hyperpolarized HDO produced by dissolution-dynamic nuclear polarization (D-DNP) is mixed with a protein solution waiting in a high-field NMR spectrometer, whereupon amide proton exchange and nuclear Overhauser effects (NOE) transfer hyperpolarization to the protein and enable acquisition of a signal-enhanced high-resolution spectrum. To date, the use of this strategy has been limited to 1D and

Identifiants

pubmed: 32040802
doi: 10.1007/s10858-020-00301-5
pii: 10.1007/s10858-020-00301-5
pmc: PMC7080779
doi:

Substances chimiques

Intrinsically Disordered Proteins 0
SPP1 protein, human 0
Ubiquitin 0
Water 059QF0KO0R
Osteopontin 106441-73-0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

161-171

Subventions

Organisme : European Research Council
ID : 339754
Pays : International
Organisme : European Research Council
ID : 279519
Pays : International
Organisme : European Research Council
ID : 801936
Pays : International
Organisme : Israel Science Foundation
ID : 965/18

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Auteurs

Gregory L Olsen (GL)

Faculty of Chemistry, Institute for Biological Chemistry, University of Vienna, Währinger Straße 38, 1090, Vienna, Austria. Gregory.Olsen@univie.ac.at.
Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel. Gregory.Olsen@univie.ac.at.

Or Szekely (O)

Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.

Borja Mateos (B)

Department of Structural and Computational Biology, University of Vienna, Vienna BioCenter 5, 1030, Vienna, Austria.

Pavel Kadeřávek (P)

CEITEC-Central European Institute of Technology, Masaryk University, Kamenice 5, 625 00, Brno, Czech Republic.
Laboratoire des biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France.

Fabien Ferrage (F)

Laboratoire des biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France.

Robert Konrat (R)

Department of Structural and Computational Biology, University of Vienna, Vienna BioCenter 5, 1030, Vienna, Austria.

Roberta Pierattelli (R)

Magnetic Resonance Center and Department of Chemistry Ugo Schiff, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, FI, Italy.

Isabella C Felli (IC)

Magnetic Resonance Center and Department of Chemistry Ugo Schiff, University of Florence, Via L. Sacconi 6, 50019, Sesto Fiorentino, FI, Italy.

Geoffrey Bodenhausen (G)

Laboratoire des biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France.

Dennis Kurzbach (D)

Faculty of Chemistry, Institute for Biological Chemistry, University of Vienna, Währinger Straße 38, 1090, Vienna, Austria. Dennis.Kurzbach@univie.ac.at.
Laboratoire des biomolécules, LBM, Département de chimie, École normale supérieure, PSL University, Sorbonne Université, CNRS, 75005, Paris, France. Dennis.Kurzbach@univie.ac.at.

Lucio Frydman (L)

Department of Chemical and Biological Physics, Weizmann Institute of Science, Rehovot, Israel.

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