A new strategy for sequential assignment of intrinsically unstructured proteins based on 15N single isotope labelling.
J Magn Reson
; 236: 1-6, 2013 Nov.
Article
en En
| MEDLINE
| ID: mdl-24018100
We describe a new efficient strategy for the sequential assignment of amide resonances of a conventional (15)N-(1)H 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.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas
/
Marcaje Isotópico
Idioma:
En
Revista:
J Magn Reson
Asunto de la revista:
DIAGNOSTICO POR IMAGEM
Año:
2013
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos