Characterization of peptide O∙∙∙HN hydrogen bonds via multidimensional 1H-detected 15N/17O solid-state nuclear magnetic resonance spectroscopy

Ivan Hung; Wenping Mao; Eric G. Keeler; Robert G. Griffin; Peter L. Gor'kov; Zhehong Gan

doi:10.26434/chemrxiv-2022-wnnz4

Physical Chemistry

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Characterization of peptide O∙∙∙HN hydrogen bonds via multidimensional 1H-detected 15N/17O solid-state nuclear magnetic resonance spectroscopy

Working Paper

Ivan Hung National High Magnetic Field Laboratory ,
Wenping Mao National High Magnetic Field Laboratory ,
Eric G. Keeler New York Structural Biology Center & Massachusetts Institute of Technology ,
Robert G. Griffin Massachusetts Institute of Technology & Francis Bitter Magnet Laboratory ,
Peter L. Gor'kov National High Magnetic Field Laboratory ,
Zhehong Gan National High Magnetic Field Laboratory

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Abstract

Solid-state NMR methods with high resolution and sensitivity are presented for identification and charaterization of hydrogen-bonded 15N/17O atomic pairs in peptide samples. Indirect 1H detection under fast magic-angle spinning, and the stronger 1H-15N and 1H-17O couplings are leveraged to significantly improve sensitivity over previous methods that use direct 15N-17O interactions.