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Expanding the membrane-protein NMR toolkit

Nature Chemical Biology volume 16, pages 937–938 (2020)Cite this article

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An NMR method to monitor conformational states of challenging large protein targets is described. The method, which can be used to evaluate distances between two labels and to measure conformational exchange rates, revealed an unanticipated outward-facing state in a glutamate transporter.

Proteins are complex machines, dynamically changing their structures to orchestrate essential biological functions1. For large membrane proteins, the toolbox to investigate these structural dynamics is not yet complete. Here, Huang et al.2 present an NMR-based method for examining structural dynamics of large membrane proteins. This method complements existing spectroscopic techniques, fills an important technical gap, and provides new insights into the dynamics of the large glutamate transporter GltPh.

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Fig. 1: 19F PRE NMR as a complement to FRET for evaluating conformational states.

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  1. Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA, USA

    Ricky C. Cheng & Merritt Maduke

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  1. Ricky C. Cheng
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  2. Merritt Maduke
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Correspondence to Merritt Maduke.

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The authors declare no competing interests.

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Cheng, R.C., Maduke, M. Expanding the membrane-protein NMR toolkit. Nat Chem Biol 16, 937–938 (2020). https://doi.org/10.1038/s41589-020-0597-7

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