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

Ruth B. Pritchard and D. Flemming Hansen ()
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Ruth B. Pritchard: University College London
D. Flemming Hansen: University College London

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-09743-4

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