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

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

doi:10.1039/D2CC07004A

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

Ivan Hung,

*^a Wenping Mao,^a Eric G. Keeler,

‡^b Robert G. Griffin,

^b Peter L. Gor'kov^a and Zhehong Gan

Author affiliations

* Corresponding authors

^a National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, Florida, USA
E-mail: hung@magnet.fsu.edu

^b Department of Chemistry and Francis Bitter Magnet Laboratory, Massachusetts Institute of Technology, Cambridge, Massachusetts, USA

Abstract

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.

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Article information

DOI: https://doi.org/10.1039/D2CC07004A
Article type: Communication
Submitted: 23 Dec 2022
Accepted: 15 Feb 2023
First published: 15 Feb 2023

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Chem. Commun., 2023,59, 3111-3113

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

I. Hung, W. Mao, E. G. Keeler, R. G. Griffin, P. L. Gor'kov and Z. Gan, Chem. Commun., 2023, 59, 3111 DOI: 10.1039/D2CC07004A

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