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Default BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.

BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.

Related Articles BSH-CP based 3D solid-state NMR experiments for protein resonance assignment.

J Biomol NMR. 2014 Mar 1;

Authors: Shi C, Fasshuber HK, Chevelkov V, Xiang S, Habenstein B, Vasa SK, Becker S, Lange A

Abstract
We have recently presented band-selective homonuclear cross-polarization (BSH-CP) as an efficient method for CO-CA transfer in deuterated as well as protonated solid proteins. Here we show how the BSH-CP CO-CA transfer block can be incorporated in a set of three-dimensional (3D) solid-state NMR (ssNMR) pulse schemes tailored for resonance assignment of proteins at high static magnetic fields and moderate magic-angle spinning rates. Due to the achieved excellent transfer efficiency of 33*% for BSH-CP, a complete set of 3D spectra needed for unambiguous resonance assignment could be rapidly recorded within 1*week for the model protein ubiquitin. Thus we expect that BSH-CP could replace the typically used CO-CA transfer schemes in well-established 3D ssNMR approaches for resonance assignment of solid biomolecules.


PMID: 24584701 [PubMed - as supplied by publisher]



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