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Optimized NMR Experiments for the Isolation of I=1/2 Manifold Transitions in Methyl Groups of Proteins

Optimized NMR Experiments for the Isolation of I=1/2 Manifold Transitions in Methyl Groups of... Optimized NMR experiments are developed for isolating magnetization belonging to the I=1/2 manifolds of 13CH3 methyl groups in proteins, enabling the manipulation of the magnetization of a 13CH3 moiety as if it were an AX (1H‐13C) spin‐system. These experiments result in the same ‘simplification’ of a 13CH3 spin‐system that would be obtained from the production of {13CHD2}‐methyl‐labeled protein samples. The sensitivity of I=1/2 manifold‐selection experiments is a factor of approximately 2 less than that of the corresponding experiments acquired on {13CHD2}‐labeled methyl groups. The methodology described here is primarily intended for small‐to‐medium sized proteins, where the losses in sensitivity associated with the isolation of I=1/2 manifold transitions can be tolerated. Several NMR applications that benefit from simplification of the 13CH3 (AX3) spin‐systems are described, with an emphasis on the measurements of methyl 1H‐13C residual dipolar couplings in a {13CH3}‐methyl‐labeled deletion mutant of the human chaperone DNAJB6b, where modulation of NMR signal intensities due to evolution of methyl 1H‐13C scalar and dipolar couplings follows a simple cosine function characteristic of an AX (1H‐13C) spin‐system, significantly simplifying data analysis. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png ChemPhysChem Wiley

Optimized NMR Experiments for the Isolation of I=1/2 Manifold Transitions in Methyl Groups of Proteins

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References (27)

Publisher
Wiley
Copyright
© 2020 Wiley‐VCH Verlag GmbH & Co. KGaA, Weinheim
ISSN
1439-4235
eISSN
1439-7641
DOI
10.1002/cphc.201900959
Publisher site
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Abstract

Optimized NMR experiments are developed for isolating magnetization belonging to the I=1/2 manifolds of 13CH3 methyl groups in proteins, enabling the manipulation of the magnetization of a 13CH3 moiety as if it were an AX (1H‐13C) spin‐system. These experiments result in the same ‘simplification’ of a 13CH3 spin‐system that would be obtained from the production of {13CHD2}‐methyl‐labeled protein samples. The sensitivity of I=1/2 manifold‐selection experiments is a factor of approximately 2 less than that of the corresponding experiments acquired on {13CHD2}‐labeled methyl groups. The methodology described here is primarily intended for small‐to‐medium sized proteins, where the losses in sensitivity associated with the isolation of I=1/2 manifold transitions can be tolerated. Several NMR applications that benefit from simplification of the 13CH3 (AX3) spin‐systems are described, with an emphasis on the measurements of methyl 1H‐13C residual dipolar couplings in a {13CH3}‐methyl‐labeled deletion mutant of the human chaperone DNAJB6b, where modulation of NMR signal intensities due to evolution of methyl 1H‐13C scalar and dipolar couplings follows a simple cosine function characteristic of an AX (1H‐13C) spin‐system, significantly simplifying data analysis.

Journal

ChemPhysChem – Wiley

Published: Mar 3, 2020

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