The measurement of binding affinities by NMR chemical shift perturbation.
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ABSTRACT:
SUBMITTER: Hobbs B
PROVIDER: S-EPMC9427925 | biostudies-literature | 2022 Aug
REPOSITORIES: biostudies-literature
Publications
The measurement of binding affinities by NMR chemical shift perturbation.
Hobbs Billy B Drant Jack J Williamson Mike P MP
Journal of biomolecular NMR 20220803 4
We have carried out chemical shift perturbation titrations on three contrasting proteins. The resulting chemical shifts have been analysed to determine the best way to fit the data, and it is concluded that a simultaneous fitting of all raw shift data to a single dissociation constant is both the most accurate and the most precise method. It is shown that the optimal weighting of <sup>15</sup>N chemical shifts to <sup>1</sup>H chemical shifts is protein dependent, but is around the consensus val ...[more]
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