A new strategy for sequential assignment of intrinsically unstructured proteins based on (15)N single isotope labelling. - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Journal of Magnetic Resonance Année : 2013

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

Résumé

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.

Domaines

Biophysique

Dates et versions

hal-00903369 , version 1 (12-11-2013)

Identifiants

Citer

Juan Lopez, Puneet Ahuja, Melanie Gerard, Jean-Michel Wieruszeski, Guy Lippens. A new strategy for sequential assignment of intrinsically unstructured proteins based on (15)N single isotope labelling.. Journal of Magnetic Resonance, 2013, 236, pp.1-6. ⟨10.1016/j.jmr.2013.07.007⟩. ⟨hal-00903369⟩

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