Title :

A new strategy for sequential assignment of intrinsically unstructured proteins based on 15N single isotope labelling

Author(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]

Journal title :

Journal of Magnetic Resonance

Volume number :

236

Pages :

1-6

Publication date :

2013-11

ISSN :

10907807

English keyword(s) :

Assignment
Intrinsically unstructured protein
NOESY
TOCSY

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [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. ...
Show more >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.Show less >

Language :

Anglais

Audience :

Non spécifiée

Administrative institution(s) :

CNRS
Université de Lille

Collections :

• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

RMN et interactions moléculaires

Submission date :

2020-02-12T15:45:00Z
2021-03-10T09:19:24Z