Characterization of peptide O⋯HN hydrogen bonds via1H-detected 15N/17O solid-state NMR spectroscopy

Characterization of peptide O⋯HN hydrogen bonds via1H-detected 15N/17O solid-state NMR spectroscopy

High sensitivity and resolution solid-state NMR methods are reported, that straightforwardly select hydrogen-bonded 15N–17O pairs from amongst all other nitrogen and oxygen sites in peptides, to aid protein secondary and tertiary structure determination. Significantly improved sensitivity is obtaine...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2023-01, 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:
Couplings
Dipoles
Hydrogen bonding
Hydrogen bonds
Nitrogen isotopes
NMR spectroscopy
Peptides
Sensitivity
Solid state
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Beschreibung
Zusammenfassung:High sensitivity and resolution solid-state NMR methods are reported, that straightforwardly select hydrogen-bonded 15N–17O 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 1H detection under fast MAS and stronger relayed dipole couplings.
ISSN:1359-7345
1364-548X
DOI:10.1039/d2cc07004a