Characterization of peptide O⋯HN hydrogen bonds via <superscript>1</superscript> H-detected <superscript>15</superscript> N/ <superscript>17</superscript> O solid-state NMR spectroscopy.
In: Chemical communications (Cambridge, England), Jg. 59 (2023-03-09), Heft 21, S. 3111-3113
academicJournal
Zugriff:
High sensitivity and resolution solid-state NMR methods are reported, that straightforwardly select hydrogen-bonded 15 N- 17 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 1 H detection under fast MAS and stronger relayed dipole couplings.
Titel: |
Characterization of peptide O⋯HN hydrogen bonds via <superscript>1</superscript> H-detected <superscript>15</superscript> N/ <superscript>17</superscript> O solid-state NMR spectroscopy.
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Autor/in / Beteiligte Person: | Hung, I ; Mao, W ; Keeler, EG ; Griffin, RG ; Gor'kov, PL ; Gan, Z |
Zeitschrift: | Chemical communications (Cambridge, England), Jg. 59 (2023-03-09), Heft 21, S. 3111-3113 |
Veröffentlichung: | Cambridge : Royal Society of Chemistry, 2023 |
Medientyp: | academicJournal |
ISSN: | 1364-548X (electronic) |
DOI: | 10.1039/d2cc07004a |
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