J 2011

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

NOVÁČEK, Jiří, Anna ZAWADZKA-KAZIMIERCZUK, Veronika PAPOUŠKOVÁ, Lukáš ŽÍDEK, Hana ŠANDEROVÁ et. al.

Basic information

Original name

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

Authors

NOVÁČEK, Jiří (203 Czech Republic, belonging to the institution), Anna ZAWADZKA-KAZIMIERCZUK (616 Poland), Veronika PAPOUŠKOVÁ (203 Czech Republic, belonging to the institution), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution), Hana ŠANDEROVÁ (203 Czech Republic), Libor KRÁSNÝ (203 Czech Republic), Wiktor KOZMINSKI (616 Poland) and Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution)

Edition

Journal of Biomolecular NMR, Dordrecht, Springer Netherlands, 2011, 0925-2738

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10610 Biophysics

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 3.612

RIV identification code

RIV/00216224:14740/11:00049942

Organization unit

Central European Institute of Technology

DOI

UT WoS

000290044400001

Keywords in English

Intrinsically disordered proteins ; Non-uniform sampling ; 13C detection ; Longitudinal relaxation optimization ; Backbone assignment

Tags

Tags

International impact, Reviewed
Změněno: 1/4/2012 06:35, Olga Křížová

Abstract

V originále

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.

Links

GAP206/11/0758, research and development project
Name: Vývoj metodologie s vysokým rozlišením pro NMR studie neuspořádaných proteinů s vysoce degenerovanými rezonančními frekvencemi (Acronym: HIGHRES)
Investor: Czech Science Foundation
GA204/09/0583, research and development project
Name: Delta podjednotka RNA polymerázy z Gram pozitivních bakterií (Acronym: DELTA)
Investor: Czech Science Foundation
GD301/09/H004, research and development project
Name: Molekulární a strukturní biologie vybraných cytostatik. Od mechanistických studií k chemoterapii rakoviny
Investor: Czech Science Foundation
LC06030, research and development project
Name: Biomolekulární centrum
Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre
MSM0021622413, plan (intention)
Name: Proteiny v metabolismu a při interakci organismů s prostředím
Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment
205872, interní kód MU
Name: Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions (Acronym: POSTBIOMIN)
Investor: European Union, Program developing interdisciplinary research POtential for the STudies of BIOMolecular INteractions, Capacities
261863, interní kód MU
Name: BioNMR Facilities - Bio NMR (Acronym: BioNMR)
Investor: European Union, Capacities