-
Something wrong with this record ?
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,
Language English Country Netherlands
Document type Journal Article, Research Support, Non-U.S. Gov't
NLK
ProQuest Central
from 1997-01-01 to 1 year ago
Medline Complete (EBSCOhost)
from 2000-01-01 to 1 year ago
Health & Medicine (ProQuest)
from 1997-01-01 to 1 year ago
- MeSH
- Bacillus subtilis enzymology MeSH
- Bacterial Proteins chemistry MeSH
- DNA-Directed RNA Polymerases chemistry MeSH
- Carbon Isotopes MeSH
- Protein Conformation MeSH
- Nuclear Magnetic Resonance, Biomolecular methods MeSH
- Proteins chemistry MeSH
- Amino Acid Sequence MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't 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.
References provided by Crossref.org
- 000
- 00000naa a2200000 a 4500
- 001
- bmc12027691
- 003
- CZ-PrNML
- 005
- 20121207111236.0
- 007
- ta
- 008
- 120817e20110320ne f 000 0#eng||
- 009
- AR
- 024 7_
- $a 10.1007/s10858-011-9496-2 $2 doi
- 035 __
- $a (PubMed)21424579
- 040 __
- $a ABA008 $b cze $d ABA008 $e AACR2
- 041 0_
- $a eng
- 044 __
- $a ne
- 100 1_
- $a Nováček, Jiří $u Faculty of Science, NCBR, and CEITEC, Masaryk University, Brno, Czech Republic.
- 245 10
- $a 5D 13C-detected experiments for backbone assignment of unstructured proteins with a very low signal dispersion / $c J. Nováček, A. Zawadzka-Kazimierczuk, V. Papoušková, L. Zídek, H. Sanderová, L. Krásný, W. Koźmiński, V. Sklenář,
- 520 9_
- $a 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.
- 650 _2
- $a sekvence aminokyselin $7 D000595
- 650 _2
- $a Bacillus subtilis $x enzymologie $7 D001412
- 650 _2
- $a bakteriální proteiny $x chemie $7 D001426
- 650 _2
- $a izotopy uhlíku $7 D002247
- 650 _2
- $a DNA řízené RNA-polymerasy $x chemie $7 D012321
- 650 _2
- $a nukleární magnetická rezonance biomolekulární $x metody $7 D019906
- 650 _2
- $a konformace proteinů $7 D011487
- 650 _2
- $a proteiny $x chemie $7 D011506
- 655 _2
- $a časopisecké články $7 D016428
- 655 _2
- $a práce podpořená grantem $7 D013485
- 700 1_
- $a Zawadzka-Kazimierczuk, Anna
- 700 1_
- $a Papoušková, Veronika
- 700 1_
- $a Zídek, Lukáš
- 700 1_
- $a Sanderová, Hana
- 700 1_
- $a Krásný, Libor
- 700 1_
- $a Koźmiński, Wiktor
- 700 1_
- $a Sklenář, Vladimír
- 773 0_
- $w MED00005454 $t Journal of biomolecular NMR $x 1573-5001 $g Roč. 50, č. 1 (20110320), s. 1-11
- 856 41
- $u https://pubmed.ncbi.nlm.nih.gov/21424579 $y Pubmed
- 910 __
- $a ABA008 $b sig $c sign $y m
- 990 __
- $a 20120817 $b ABA008
- 991 __
- $a 20121207111311 $b ABA008
- 999 __
- $a ok $b bmc $g 949733 $s 785037
- BAS __
- $a 3
- BAS __
- $a PreBMC
- BMC __
- $a 2011 $b 50 $c 1 $d 1-11 $e 20110320 $i 1573-5001 $m Journal of biomolecular NMR $n J Biomol NMR $x MED00005454
- LZP __
- $a Pubmed-20120817/11/03
