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5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion

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NOVÁČEK Jiří ZAWADZKA-KAZIMIERCZUK Anna PAPOUŠKOVÁ Veronika ŽÍDEK Lukáš ŠANDEROVÁ Hana KRÁSNÝ Libor KOZMINSKI Wiktor SKLENÁŘ Vladimír

Rok publikování 2011
Druh Článek v odborném periodiku
Časopis / Zdroj Journal of Biomolecular NMR
Fakulta / Pracoviště MU

Středoevropský technologický institut

Citace
Doi http://dx.doi.org/10.1007/s10858-011-9496-2
Obor Biofyzika
Klíčová slova Intrinsically disordered proteins ; Non-uniform sampling ; 13C detection ; Longitudinal relaxation optimization ; Backbone assignment
Popis Two novel 5D NMR experiments (CACONCACO, NCOCANCO) for backbone assignment of disordered proteins are presented. The pulse sequences exploit relaxation properties of the unstructured proteins and combine the advantages of 13C-direct detection, non-uniform sampling, and longitudinal relaxation optimization to maximize the achievable resolution and minimize the experimental time. The pulse sequences were successfully tested on the sample of partially disordered delta subunit from RNA polymerase from Bacillus subtilis. The unstructured part of this 20 kDa protein consists of 81 amino acids with frequent sequential repeats. A collection of 0.0003% of the data needed for a conventional experiment with linear sampling was sufficient to perform an unambiguous assignment of the disordered part of the protein from a single 5D spectrum.
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