Characterization of peptide O⋯HN hydrogen bonds via1H-detected 15N/17O solid-state NMR spectroscopy
Name
nihms-1877290.pdf
Description
Accepted version
Size
471.03 KB
Format
Adobe PDF
Checksum (MD5)
5466ae2077bac39314138f8ceae5f203
Author(s) • • • • •
Hung, Ivan
Mao, Wenping
Keeler, Eric G
Griffin, Robert G
Gor'kov, Peter L
Gan, Zhehong
Date Issued
February 15, 2023
Journal
Chemical Communications
Publisher
Royal Society of Chemistry
Citation
Ivan Hung, Wenping Mao, Eric G. Keeler, Robert G. Griffin, Peter L. Gor'kov, Zhehong Gan; Characterization of peptide O⋯HN hydrogen bonds via1H-detected 15N/17O solid-state NMR spectroscopy. Chem. Commun. 2023; 59 (21): 3111–3113.
Version
Author's final manuscript
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.
Terms of Use
Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use.
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1039/d2cc07004a