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

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Sensitive and simplified : a combinatorial acquisition of five distinct 2D constant-time 13C− 1H NMR protein correlation spectra. / Yoshimura, Yuichi; Mulder, Frans A. A.

In: Journal of Biomolecular NMR, Vol. 74, No. 12, 12.2020, p. 695-706.

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@article{06f521378c754ee8af10602591d7be5a,
title = "Sensitive and simplified: a combinatorial acquisition of five distinct 2D constant-time 13C− 1H NMR protein correlation spectra",
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 β− 1H β correlations of asparagine and aspartic acid, 13C γ− 1H γ correlations of glutamine and glutamic acid, and 13C α− 1H α correlations of glycine, (ii) 13C α− 1H α correlations of all residues but glycine, and (iii) 13C β− 1H 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. ",
keywords = "C-13 chemical shifts, Constant-time HSQC, Multiplicity editing, Scalar coupling, Selective observation, HETERONUCLEAR SHIFT-CORRELATION, SELECTIVE H-1-N-15 CORRELATIONS, TRIPLE-RESONANCE EXPERIMENTS, SPIN-SYSTEM TOPOLOGIES, DEPT SEQUENCE, C-H, ACID, ASSIGNMENT, MUSIC, SPECTROSCOPY, C chemical shifts",
author = "Yuichi Yoshimura and Mulder, {Frans A. A.}",
year = "2020",
month = dec,
doi = "10.1007/s10858-020-00341-x",
language = "English",
volume = "74",
pages = "695--706",
journal = "Journal of Biomolecular N M R",
issn = "0925-2738",
publisher = "Springer",
number = "12",

}

RIS

TY - JOUR

T1 - Sensitive and simplified

T2 - a combinatorial acquisition of five distinct 2D constant-time 13C− 1H NMR protein correlation spectra

AU - Yoshimura, Yuichi

AU - Mulder, Frans A. A.

PY - 2020/12

Y1 - 2020/12

N2 - 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 β− 1H β correlations of asparagine and aspartic acid, 13C γ− 1H γ correlations of glutamine and glutamic acid, and 13C α− 1H α correlations of glycine, (ii) 13C α− 1H α correlations of all residues but glycine, and (iii) 13C β− 1H 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.

AB - 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 β− 1H β correlations of asparagine and aspartic acid, 13C γ− 1H γ correlations of glutamine and glutamic acid, and 13C α− 1H α correlations of glycine, (ii) 13C α− 1H α correlations of all residues but glycine, and (iii) 13C β− 1H 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.

KW - C-13 chemical shifts

KW - Constant-time HSQC

KW - Multiplicity editing

KW - Scalar coupling

KW - Selective observation

KW - HETERONUCLEAR SHIFT-CORRELATION

KW - SELECTIVE H-1-N-15 CORRELATIONS

KW - TRIPLE-RESONANCE EXPERIMENTS

KW - SPIN-SYSTEM TOPOLOGIES

KW - DEPT SEQUENCE

KW - C-H

KW - ACID

KW - ASSIGNMENT

KW - MUSIC

KW - SPECTROSCOPY

KW - C chemical shifts

U2 - 10.1007/s10858-020-00341-x

DO - 10.1007/s10858-020-00341-x

M3 - Journal article

C2 - 32804297

VL - 74

SP - 695

EP - 706

JO - Journal of Biomolecular N M R

JF - Journal of Biomolecular N M R

SN - 0925-2738

IS - 12

ER -