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Pure shift amide detection in conventional and TROSY-type experiments of 13C,15N-labeled proteins

Haller, Jens D. 1; Bodor, Andrea; Luy, Burkhard ORCID iD icon 1
1 Institut für Organische Chemie (IOC), Karlsruher Institut für Technologie (KIT)

Abstract:

Large coupling networks in uniformly 13C,15N-labeled biomolecules induce broad multiplets that even in flexible proteins are frequently not recognized as such. The reason is that given multiplets typically consist of a large number of individual resonances that result in a single broad line, in which individual components are no longer resolved. We here introduce a real-time pure shift acquisition scheme for the detection of amide protons which is based on 13C-BIRDr,X. As a result the full homo- and heteronuclear coupling network can be suppressed at low power leading to real singlets at substantially improved resolution and uncompromised sensitivity. The method is tested on a small globular and an intrinsically disordered protein (IDP) where the average spectral resolution is increased by a factor of ~ 2 and higher. Equally important, the approach works without saturation of water magnetization for solvent suppression and exchanging amide protons are not affected by saturation transfer.

Zugehörige Institution(en) am KIT Institut für Organische Chemie (IOC)
Publikationstyp Zeitschriftenaufsatz
Publikationsmonat/-jahr 12.2022
Sprache Englisch
Identifikator ISSN: 0925-2738, 1573-5001
KITopen-ID: 1000153822
HGF-Programm 43.35.02 (POF IV, LK 01) Functionality of Soft Matter and Biomolecular Systems
Erschienen in Journal of Biomolecular NMR
Verlag Springer
Band 76
Heft 5-6
Seiten 213–221
Vorab online veröffentlicht am 18.11.2022
Nachgewiesen in Web of Science
Dimensions
Scopus
OpenAlex
Globale Ziele für nachhaltige Entwicklung Ziel 6 – Sauberes Wasser und Sanitär-Einrichtungen

Verlagsausgabe §
DOI: 10.5445/IR/1000153822
Veröffentlicht am 13.12.2022
Originalveröffentlichung
DOI: 10.1007/s10858-022-00406-z
Scopus
Zitationen: 3
Web of Science
Zitationen: 1
Dimensions
Zitationen: 4
Seitenaufrufe: 80
seit 14.12.2022
Downloads: 55
seit 15.12.2022
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