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5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion
J. Nováček, A. Zawadzka-Kazimierczuk, V. Papoušková, L. Zídek, H. Sanderová, L. Krásný, W. Koźmiński, V. Sklenář,
Jazyk angličtina Země Nizozemsko
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
ProQuest Central
od 1997-01-01 do Před 1 rokem
Medline Complete (EBSCOhost)
od 2000-01-01 do Před 1 rokem
Health & Medicine (ProQuest)
od 1997-01-01 do Před 1 rokem
- MeSH
- Bacillus subtilis enzymologie MeSH
- bakteriální proteiny chemie MeSH
- DNA řízené RNA-polymerasy chemie MeSH
- izotopy uhlíku MeSH
- konformace proteinů MeSH
- nukleární magnetická rezonance biomolekulární metody MeSH
- proteiny chemie MeSH
- sekvence aminokyselin MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
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 (13)C-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.
Citace poskytuje Crossref.org
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