A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR

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A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR

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11-01-2017, 05:51 AM

nmrlearner

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A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR

A robust heteronuclear dipolar recoupling method comparable to TEDOR for proteins in magic-angle spinning solid-state NMR

Publication date: Available online 31 October 2017
Source:Journal of Magnetic Resonance

Author(s): Zhengfeng Zhang, Jianping Li, Yanke Chen, Huayong Xie, Jun Yang

In this letter, we propose a robust heteronuclear dipolar recoupling method for proteins in magic-angle spinning (MAS) solid-state NMR. This method is as simple, robust and efficient as the well-known TEDOR in the aspect of magnetization transfer between 15N and 13C. Deriving from our recent band-selective dual back-to-back pulses (DBP) (J. Magn. Reson., 2016, 272, 46-52), this method uses new phase-cycling schemes to realize broadband DBP (Bro-DBP). For broadband 15N-13C magnetization transfer (simultaneous 15N->13C? and 15N->13C?), Bro-DBP has almost the same 15N->13C? efficiency while offers 30% - 40% enhancement on 15N->13C? transfer, compared to TEDOR. Besides, Bro-DBP can also be used as a carbonyl (13C?)-selected method, whose 15N->13C? efficiency is up to 1.7 times that of TEDOR and is also higher than that of band-selective DBP. The performance of Bro-DBP is demonstrated on the N-formyl-[U-13C,15N]-Met-Leu-Phe-OH (fMLF) peptide and the U-13C, 15N labeled ?1 immunoglobulin binding domain of protein G (GB1) microcrystalline protein. Since Bro-DBP is as robust, simple and efficient as TEDOR, we believe it is very useful for protein studies in MAS solid-state NMR.
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