4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins

NOVÁČEK, Jiří, Noam Y HABA, Jordan H CHILL, Lukáš ŽÍDEK and Vladimír SKLENÁŘ. 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins. Online. Journal of Biomolecular NMR. Dordrecht: Springer Netherlands, 2012, vol. 53, No 2, p. 139-148. ISSN 0925-2738. Available from: https://dx.doi.org/10.1007/s10858-012-9631-8. [citováno 2024-04-23]

Basic information

• Original name: 4D Non-uniformly sampled HCBCACON and (1) J(NC alpha)-selective HCBCANCO experiments for the sequential assignment and chemical shift analysis of intrinsically disordered proteins
• Authors: NOVÁČEK, Jiří (203 Czech Republic, belonging to the institution), Noam Y HABA (376 Israel), Jordan H CHILL (376 Israel), Lukáš ŽÍDEK (203 Czech Republic, guarantor, belonging to the institution) and Vladimír SKLENÁŘ (203 Czech Republic, belonging to the institution)
• Edition: Journal of Biomolecular NMR, Dordrecht, Springer Netherlands, 2012, 0925-2738.

Other information

• Original language: English
• Type of outcome: Article in a journal
• Field of Study: 10610 Biophysics
• Country of publisher: Netherlands
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Impact factor: Impact factor: 2.845
• RIV identification code: RIV/00216224:14740/12:00057624
• Organization unit: Central European Institute of Technology
• Doi: http://dx.doi.org/10.1007/s10858-012-9631-8
• UT WoS: 000305943400007
• Keywords in English: Intrinsically disordered proteins; Non-uniform sampling; C-13 detection; Chemical shifts; Residual secondary structure; Prolines assignment
• Tags: ok, rivok

Abstract

A pair of 4D NMR experiments for the backbone assignment of disordered proteins is presented. The experiments exploit C-13 direct detection and non-uniform sampling of the indirectly detected dimensions, and provide correlations of the aliphatic proton (H-alpha, and H-beta) and carbon (C-alpha, C-beta) resonance frequencies to the protein backbone. Thus, all the chemical shifts regularly used to map the transient secondary structure motifs in the intrinsically disordered proteins (H-alpha, C-alpha, C-beta, C', and N) can be extracted from each spectrum. Compared to the commonly used assignment strategy based on matching the C-alpha and C-beta chemical shifts, inclusion of the H-alpha and H-beta provides up to three extra resonance frequencies that decrease the chance of ambiguous assignment. The experiments were successfully applied to the original assignment of a 12.8 kDa intrinsically disordered protein having a high content of proline residues (26 %) in the sequence.

Links

• ED1.1.00/02.0068, research and development project: Name: CEITEC - central european institute of technology
• 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

• 228461, interní kód MU: Name: Enhancing Access and Services to East European users Towards an efficient (Acronym: EAST-NMR)

Investor: European Union, Enhancing Access and Services to East European users Towards an efficient, Capacities