Afficher la couverture 'Spectral editing of intra- and inter-chain methyl–methyl NOEs in protein complexes | Törner, Ricarda' en grand format
/5

0 avis

Spectral editing of intra- and inter-chain methyl–methyl NOEs in protein complexes

Archive ouverte

Törner, Ricarda | Awad, Rida | Gans, Pierre | Brutscher, Bernhard | Boisbouvier, Jérôme

Edité par CCSD ; Springer Verlag -

International audience. Specific isotopic labeling of methyl groups in a perdeuterated protein background enables the detection of long range NOEs in proteins or high molecular weight complexes. We introduce here an approach, combining an optimized isotopic labeling scheme with a specifically tailored NMR pulse sequence, to distinguish between intramolecular and intermolecular NOE connectivities. In hetero-oligomeric complexes, this strategy enables sign encoding of intra-subunit and inter-subunit NOEs. For homo-oligomeric assemblies, our strategy allows the specific detection of intra-chain NOEs in high resolution 3D NOESY spectra. The general principles, possibilities and limitations of this approach are presented. Applications of this approach for the detection of intermolecular NOEs in a hetero-hexamer, and the assignment of methyl 1H and 13C resonances in a homo-tetrameric protein complex are shown.

Suggestions

Du même auteur

Backbone and methyl resonances assignment of the 87 kDa prefoldin from Pyrococcus horikoshii

Archive ouverte | Törner, Ricarda | CCSD

International audience. Prefoldin is a heterohexameric protein assembly which acts as a co-chaperonin for the well conserved Hsp60 chaperonin, present in archaebacteria and the eukaryotic cell cytosol. Prefoldin is ...

Optimized precursor to simplify assignment transfer between backbone resonances and stereospecifically labelled valine and leucine methyl groups: application to human Hsp90 N-terminal domain

Archive ouverte | Henot, Faustine | CCSD

International audience. Methyl moieties are highly valuable probes for quantitative NMR studies of large proteins. Hence, their assignment is of the utmost interest to obtain information on both interactions and dyn...

Structural basis for the inhibition of IAPP fibril formation by the co-chaperonin prefoldin

Archive ouverte | Törner, Ricarda | CCSD

International audience. Chaperones, as modulators of protein conformational states, are key cellular actors to prevent the accumulation of fibrillar aggregates. Here, we integrated kinetic investigations with struct...

Chargement des enrichissements...