Characterization of peptide O⋯HN hydrogen bonds via 1 H-detected 15 N/ 17 O solid-state NMR spectroscopy

Characterization of peptide O⋯HN hydrogen bonds via 1 H-detected 15 N/ 17 O solid-state NMR spectroscopy

High sensitivity and resolution solid-state NMR methods are reported, that straightforwardly select hydrogen-bonded N- O pairs from amongst all other nitrogen and oxygen sites in peptides, to aid protein secondary and tertiary structure determination. Significantly improved sensitivity is obtained w...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2023-03, Vol.59 (21), p.3111-3113
Hauptverfasser: Hung, Ivan, Mao, Wenping, Keeler, Eric G, Griffin, Robert G, Gor'kov, Peter L, Gan, Zhehong
Format: Artikel
Sprache:eng
Schlagworte:
Hydrogen Bonding
Magnetic Resonance Spectroscopy - methods
Nitrogen
Peptides - chemistry
Proteins - chemistry
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Beschreibung
Zusammenfassung:High sensitivity and resolution solid-state NMR methods are reported, that straightforwardly select hydrogen-bonded N- O pairs from amongst all other nitrogen and oxygen sites in peptides, to aid protein secondary and tertiary structure determination. Significantly improved sensitivity is obtained with indirect H detection under fast MAS and stronger relayed dipole couplings.
ISSN:1359-7345
1364-548X
DOI:10.1039/d2cc07004a