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Optimized NMR Experiments for the Isolation of I = ½ Manifold Transitions in Methyl Groups of Proteins.

07:00 EST 8th November 2019 | BioPortfolio

Summary of "Optimized NMR Experiments for the Isolation of I = ½ Manifold Transitions in Methyl Groups of Proteins."

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 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.

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Name: Chemphyschem : a European journal of chemical physics and physical chemistry
ISSN: 1439-7641
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