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

27 December 2022, Version 1
Working Paper
This content is a preprint and has not undergone peer review at the time of posting.

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.

Keywords

17O
15N
hydrogen-bond
multidimensional NMR
distance measurement
1H detection
solid-state NMR

Supplementary materials

Title
Description
Actions
Title
Additional experimental details.
Description
Detailed solid-state NMR experimental parameters and schematic pulse sequences for the OhNH experiments.
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Now Published

Characterization of peptide O∙∙∙HN hydrogen bonds via 1H-detected 15N/17O solid-state NMR spectroscopy [opens in a new tab]
Ivan Hung, Wenping Mao, Eric G. Keeler, Robert G. Griffin, Peter Gor'kov, Zhehong Gan journal article
Chemical Communications
Online publication date: 2023

Version History

Dec 27, 2022 Version 1

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The content is available under CC BY NC ND 4.0 [opens in a new tab]

DOI

10.26434/chemrxiv-2022-wnnz4
D O I: 10.26434/chemrxiv-2022-wnnz4 [opens in a new tab]

Funding

Division of Materials Research
DMR-1644779
National Institutes of Health
AG058504
National Institutes of Health
GM132997
National Institutes of Health
GM132079

Author’s competing interest statement

The author(s) have declared they have no conflict of interest with regard to this content

Ethics

The author(s) declare that they have sought and gained approval from the relevant ethics committee/IRB for this research and its publication.

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