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Super resolution NOESY spectra of proteins

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Abstract

Spectral resolution remains one of the most significant limitations in the NMR study of biomolecules. We present the srNOESY (super resolution nuclear overhauser effect spectroscopy) experiment, which enhances the resolution of NOESY cross-peaks at the expense of the diagonal peak line-width. We studied two proteins, ubiquitin and the influenza hemagglutinin fusion peptide in bicelles, and we achieved average resolution enhancements of 21–47% and individual peak enhancements as large as ca. 450%. New peaks were observed over the conventional NOESY experiment in both proteins as a result of these improvements, and the final structures generated from the calculated restraints matched published models. We discuss the impact of the experimental parameters, spin diffusion and the information content of the srNOESY lineshape.

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Acknowledgements

This work was supported by the National Science Foundation under Grant No. 1651598 and funds from the Department of Chemistry at the University of Illinois at Chicago. This study made use of NMRbox: National Center for Biomolecular NMR Data Processing and Analysis, a Biomedical Technology Research Resource (BTRR), which is supported by NIH Grant P41GM111135 (NIGMS).

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  1. Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL, 60607, USA

    Charles F. DeLisle, H. Bhagya Mendis & Justin L. Lorieau

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  1. Charles F. DeLisle
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  2. H. Bhagya Mendis
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  3. Justin L. Lorieau
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Correspondence to Justin L. Lorieau.

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DeLisle, C.F., Mendis, H.B. & Lorieau, J.L. Super resolution NOESY spectra of proteins. J Biomol NMR 73, 105–116 (2019). https://doi.org/10.1007/s10858-019-00231-x

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