Exclusively heteronuclear NMR experiments for the investigation of intrinsically disordered proteins: focusing on proline residues.


Journal

Magnetic resonance (Gottingen, Germany)
ISSN: 2699-0016
Titre abrégé: Magn Reson (Gott)
Pays: Germany
ID NLM: 101775538

Informations de publication

Date de publication:
2021
Historique:
received: 27 03 2021
accepted: 02 06 2021
medline: 1 7 2021
pubmed: 1 7 2021
entrez: 31 10 2023
Statut: epublish

Résumé

NMR represents a key spectroscopic technique that contributes to the emerging field of highly flexible, intrinsically disordered proteins (IDPs) or protein regions (IDRs) that lack a stable three-dimensional structure. A set of exclusively heteronuclear NMR experiments tailored for proline residues, highly abundant in IDPs/IDRs, are presented here. They provide a valuable complement to the widely used approach based on amide proton detection, filling the gap introduced by the lack of amide protons in proline residues within polypeptide chains. The novel experiments have very interesting properties for the investigations of IDPs/IDRs of increasing complexity.

Identifiants

pubmed: 37904768
doi: 10.5194/mr-2-511-2021
pii: 01021829
pmc: PMC10539766
doi:

Types de publication

Journal Article

Langues

eng

Pagination

511-522

Informations de copyright

Copyright: © 2021 Isabella C. Felli et al.

Déclaration de conflit d'intérêts

The authors declare that they have no conflict of interest.

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Auteurs

Isabella C Felli (IC)

CERM and Department of Chemistry "Ugo Schiff", University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.

Wolfgang Bermel (W)

Bruker BioSpin GmbH, Silberstreifen 4, 76287 Rheinstetten, Germany.

Roberta Pierattelli (R)

CERM and Department of Chemistry "Ugo Schiff", University of Florence, Via Luigi Sacconi 6, 50019 Sesto Fiorentino, Florence, Italy.

Classifications MeSH