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Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy

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  • Ruth B. Pritchard

    (University College London)

  • D. Flemming Hansen

    (University College London)

Abstract

Side chains cover protein surfaces and are fundamental to processes as diverse as substrate recognition, protein folding and enzyme catalysis. However, characterisation of side-chain motions has so far been restricted to small proteins and methyl-bearing side chains. Here we present a class of methods, based on 13C-detected NMR spectroscopy, to more generally quantify motions and interactions of side chains in medium-to-large proteins. A single, uniformly isotopically labelled sample is sufficient to characterise the side chains of six different amino acid types. Side-chain conformational dynamics on the millisecond time-scale can be quantified by incorporating chemical exchange saturation transfer (CEST) into the presented methods, whilst long-range 13C-13C scalar couplings reporting on nanosecond to millisecond motions can be quantified in proteins as large as 80 kDa. The presented class of methods promises characterisation of side-chain behaviour at a level that has so far been reserved for the protein backbone.

Suggested Citation

  • Ruth B. Pritchard & D. Flemming Hansen, 2019. "Characterising side chains in large proteins by protonless 13C-detected NMR spectroscopy," Nature Communications, Nature, vol. 10(1), pages 1-7, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09743-4
    DOI: 10.1038/s41467-019-09743-4
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    Cited by:

    1. Gogulan Karunanithy & Vaibhav Kumar Shukla & D. Flemming Hansen, 2024. "Solution-state methyl NMR spectroscopy of large non-deuterated proteins enabled by deep neural networks," Nature Communications, Nature, vol. 15(1), pages 1-12, December.

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