| BLAHUT, Jan, Matthias J BRANDL, Tejaswini PRADHAN, Bernd REIF and Zdenek TOSNER. Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences. Journal of the American Chemical Society. Washington: American Chemical Society, 2022, vol. 144, No 38, p. 17336-17340. ISSN 0002-7863. Available from: https://dx.doi.org/10.1021/jacs.2c06568. |
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@article{2267727,
author = {Blahut, Jan and Brandl, Matthias J and Pradhan, Tejaswini and Reif, Bernd and Tosner, Zdenek},
article_location = {Washington},
article_number = {38},
doi = {http://dx.doi.org/10.1021/jacs.2c06568},
keywords = {Carbon; Humans; Immunoglobulin Light Chains; Magnetic Resonance Spectroscopy; Nuclear Magnetic Resonance; Biomolecular; Proteins; Protons},
language = {eng},
issn = {0002-7863},
journal = {Journal of the American Chemical Society},
title = {Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences},
url = {https://pubs.acs.org/doi/10.1021/jacs.2c06568},
volume = {144},
year = {2022}
}
TY - JOUR
ID - 2267727
AU - Blahut, Jan - Brandl, Matthias J - Pradhan, Tejaswini - Reif, Bernd - Tosner, Zdenek
PY - 2022
TI - Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences
JF - Journal of the American Chemical Society
VL - 144
IS - 38
SP - 17336-17340
EP - 17336-17340
PB - American Chemical Society
SN - 00027863
KW - Carbon
KW - Humans
KW - Immunoglobulin Light Chains
KW - Magnetic Resonance Spectroscopy
KW - Nuclear Magnetic Resonance
KW - Biomolecular
KW - Proteins
KW - Protons
UR - https://pubs.acs.org/doi/10.1021/jacs.2c06568
N2 - Recently, proton-detected magic-angle spinning (MAS) solid-state nuclear magnetic resonance (NMR) spectroscopy has become an attractive tool to study the structure and dynamics of insoluble proteins at atomic resolution. The sensitivity of the employed multidimensional experiments can be systematically improved when both transversal components of the magnetization are transferred simultaneously after an evolution period. The method of preservation of equivalent pathways has been explored in solution-state NMR; however, it does not find widespread application due to relaxation issues connected with increased molecular size. We present here for the first time heteronuclear transverse mixing sequences for correlation experiments at moderate and fast MAS frequencies. Optimal control allows to boost the signal-to-noise ratio (SNR) beyond the expected factor of root 2 for each indirect dimension. In addition to the carbon-detected sensitivity-enhanced 2D NCA experiment, we present a novel proton detected, doubly sensitivity-enhanced 3D hCANH pulse sequence for which we observe a 3-fold improvement in SNR compared to the conventional experimental implementation. The sensitivity gain turned out to be essential to unambiguously characterize a minor fibril polymorph of a human lambda-III immunoglobulin light chain protein that escaped detection so far.
ER -
BLAHUT, Jan, Matthias J BRANDL, Tejaswini PRADHAN, Bernd REIF and Zdenek TOSNER. Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences. \textit{Journal of the American Chemical Society}. Washington: American Chemical Society, 2022, vol.~144, No~38, p.~17336-17340. ISSN~0002-7863. Available from: https://dx.doi.org/10.1021/jacs.2c06568.
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