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5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion
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SYSNO ASEP 0367828 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název 5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion Tvůrce(i) Nováček, J. (CZ)
Zawadzka-Kazimierczuk, A. (PL)
Papoušková, V. (CZ)
Žídek, L. (CZ)
Šanderová, Hana (MBU-M) RID, ORCID
Krásný, Libor (MBU-M) RID, ORCID
Kozminski, W. (PL)
Sklenář, V. (CZ)Zdroj.dok. Journal of Biomolecular NMR - ISSN 0925-2738
Roč. 50, č. 1 (2011), s. 1-11Poč.str. 11 s. Jazyk dok. eng - angličtina Země vyd. NL - Nizozemsko Klíč. slova Intrinsically disordered proteins ; Non-uniform sampling ; Longitudinal relaxation optimization Vědní obor RIV EE - Mikrobiologie, virologie CEP GA204/09/0583 GA ČR - Grantová agentura ČR CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000290044400001 DOI 10.1007/s10858-011-9496-2 Anotace 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 Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2012
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