Studying Intrinsically Disordered Proteins ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
Studying Intrinsically Disordered Proteins under True In Vivo Conditions by Combined Cross-Polarization and Carbonyl-Detection NMR Spectroscopy
Author(s) :
Lopez, Juan [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Pontificia Universidad Católica del Perú = Pontifical Catholic University of Peru [PUCP]
Schneider, Robert [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Cantrelle, Francois-Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Huvent, Isabelle [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Pontificia Universidad Católica del Perú = Pontifical Catholic University of Peru [PUCP]
Schneider, Robert [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Cantrelle, Francois-Xavier [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Huvent, Isabelle [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle UMR 8576 [UGSF]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés [LISBP]
Journal title :
Angewandte Chemie International Edition
Volume number :
55
Pages :
7418-7422
Publication date :
2016-06-20
ISSN :
1433-7851
English keyword(s) :
Alpha-synuclein
Carbon detection
Cross-polarization
In-cell NMR spectroscopy
Intrinsically disordered proteins
Carbon detection
Cross-polarization
In-cell NMR spectroscopy
Intrinsically disordered proteins
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [en]
Under physiological conditions, studies of intrinsically disordered proteins (IDPs) by conventional NMR methods based on proton detection are severely limited by fast amide‐proton exchange with water. 13C detection has ...
Show more >Under physiological conditions, studies of intrinsically disordered proteins (IDPs) by conventional NMR methods based on proton detection are severely limited by fast amide‐proton exchange with water. 13C detection has been proposed as a solution to the exchange problem, but is hampered by low sensitivity. We propose a new pulse sequence combining proton–nitrogen cross‐polarization and carbonyl detection to record high‐resolution, high‐sensitivity NMR spectra of IDPs under physiological conditions. To demonstrate the efficacy of this approach, we recorded a high‐quality N–CO correlation spectrum of α‐synuclein in bacterial cells at 37 °C.Show less >
Show more >Under physiological conditions, studies of intrinsically disordered proteins (IDPs) by conventional NMR methods based on proton detection are severely limited by fast amide‐proton exchange with water. 13C detection has been proposed as a solution to the exchange problem, but is hampered by low sensitivity. We propose a new pulse sequence combining proton–nitrogen cross‐polarization and carbonyl detection to record high‐resolution, high‐sensitivity NMR spectra of IDPs under physiological conditions. To demonstrate the efficacy of this approach, we recorded a high‐quality N–CO correlation spectrum of α‐synuclein in bacterial cells at 37 °C.Show less >
Language :
Anglais
Audience :
Non spécifiée
ANR Project :
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Research team(s) :
RMN et interactions moléculaires
Submission date :
2020-02-12T15:44:52Z
2021-04-23T08:45:55Z
2021-04-23T08:45:55Z