A new strategy for sequential assignment ...
Type de document :
Article dans une revue scientifique
URL permanente :
Titre :
A new strategy for sequential assignment of intrinsically unstructured proteins based on 15N single isotope labelling
Auteur(s) :
Lopez, Juan [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ahuja, Puneet [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Gerard, Melanie [Auteur]
Catholic University of Leuven = Katholieke Universiteit Leuven [KU Leuven]
Wieruszeski, Jean-Michel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Ahuja, Puneet [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Gerard, Melanie [Auteur]
Catholic University of Leuven = Katholieke Universiteit Leuven [KU Leuven]
Wieruszeski, Jean-Michel [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lippens, Guy [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Titre de la revue :
Journal of Magnetic Resonance
Numéro :
236
Pagination :
1-6
Date de publication :
2013-11
ISSN :
10907807
Mot(s)-clé(s) en anglais :
Assignment
Intrinsically unstructured protein
NOESY
TOCSY
Intrinsically unstructured protein
NOESY
TOCSY
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
We describe a new efficient strategy for the sequential assignment of amide resonances of a conventional 15N–1H HSQC spectrum of intrinsically unfolded proteins, based on composite NOESY–TOCSY and TOCSY–NOESY mixing times. ...
Lire la suite >We describe a new efficient strategy for the sequential assignment of amide resonances of a conventional 15N–1H HSQC spectrum of intrinsically unfolded proteins, based on composite NOESY–TOCSY and TOCSY–NOESY mixing times. These composite mixing times lead to a Hα-proton mediated unidirectional transfer of amide to amide proton. We have implemented the composite mixing times in an HSQC–NOESY–HSQC manner to obtain directional connectivity between amides of neighbouring residues. We experimentally determine the optimal mixing times for both transfer schemes, and demonstrate its use in the assignment for both a fragment of the neuronal tau protein and for α-synuclein.Lire moins >
Lire la suite >We describe a new efficient strategy for the sequential assignment of amide resonances of a conventional 15N–1H HSQC spectrum of intrinsically unfolded proteins, based on composite NOESY–TOCSY and TOCSY–NOESY mixing times. These composite mixing times lead to a Hα-proton mediated unidirectional transfer of amide to amide proton. We have implemented the composite mixing times in an HSQC–NOESY–HSQC manner to obtain directional connectivity between amides of neighbouring residues. We experimentally determine the optimal mixing times for both transfer schemes, and demonstrate its use in the assignment for both a fragment of the neuronal tau protein and for α-synuclein.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Équipe(s) de recherche :
RMN et interactions moléculaires
Date de dépôt :
2020-02-12T15:45:00Z
2021-03-10T09:19:24Z
2021-03-10T09:19:24Z