[NMR paper] 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.

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

J Magn Reson. 2017 Oct 31;285:79-85

Authors: Zhang Z, Li J, Chen Y, Xie H, Yang J

Abstract
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 (15)N and (13)C. Deriving from our recent band-selective dual back-to-back pulses (DBP) (Zhang et al., 2016), this method uses new phase-cycling schemes to realize broadband DBP (Bro-DBP). For broadband (15)N-(13)C magnetization transfer (simultaneous (15)N->(13)C' and (15)N->(13)C?), Bro-DBP has almost the same (15)N->(13)C? efficiency while offers 30-40% enhancement on (15)N->(13)C' transfer, compared to TEDOR. Besides, Bro-DBP can also be used as a carbonyl ((13)C')-selected method, whose (15)N->(13)C' 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-(13)C,(15)N]-Met-Leu-Phe-OH (fMLF) peptide and the U-(13)C, (15)N 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.


PMID: 29126001 [PubMed - as supplied by publisher]



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