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
SN - 0925-2738
VL - 74
SP - 695
EP - 706
JO - Journal of Biomolecular NMR
JF - Journal of Biomolecular NMR
IS - 12
ER -