Sensitive and simplified: a combinatorial acquisition of five distinct 2D constant-time 13C− 1H NMR protein correlation spectra

Yuichi Yoshimura, Frans A. A. Mulder*

*Corresponding author af dette arbejde

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Abstract

A procedure is presented for the substantial simplification of 2D constant-time 13C− 1H heteronuclear single-quantum correlation (HSQC) spectra of 13C-enriched proteins. In this approach, a single pulse sequence simultaneously records eight sub-spectra wherein the phases of the NMR signals depend on spin topology. Signals from different chemical groups are then stratified into different sub-spectra through linear combination based on Hadamard encoding of 13CH n multiplicity (n = 1, 2, and 3) and the chemical nature of neighboring 13C nuclei (aliphatic, carbonyl/carboxyl, aromatic). This results in five sets of 2D NMR spectra containing mutually exclusive signals from: (i) 13C β1H β correlations of asparagine and aspartic acid, 13C γ1H γ correlations of glutamine and glutamic acid, and 13C α1H α correlations of glycine, (ii) 13C α1H α correlations of all residues but glycine, and (iii) 13C β1H β correlations of phenylalanine, tyrosine, histidine, and tryptophan, and the remaining (iv) aliphatic 13CH 2 and (v) aliphatic 13CH/ 13CH 3 resonances. As HSQC is a common element of many NMR experiments, the spectral simplification proposed in this article can be straightforwardly implemented in experiments for resonance assignment and structure determination and should be of widespread utility.

OriginalsprogEngelsk
TidsskriftJournal of Biomolecular NMR
Vol/bind74
Nummer12
Sider (fra-til)695-706
ISSN0925-2738
DOI
StatusUdgivet - dec. 2020

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