Abstract
NMR diffusion coefficient measurements have been shown to be sensitive to the conformational and oligomeric states of proteins. Recently, heteronuclear-filtered diffusion experiments have been proposed [Dingley et al. (1997) J. Biomol. NMR, 10, 1–8]. Several new heteronuclear-filtered diffusion pulse sequences are proposed which are shown to have superior sensitivity to those previously proposed. One of these new heteronuclear-filtered diffusion experiments has been used to study the binding of an SH3 domain to a peptide. Using this system, we show that it is possible to measure binding constants from diffusion coefficient measurements.
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Tillett, M.L., Horsfield, M.A., Lian, LY. et al. Protein-ligand interactions measured by 15N-filtered diffusion experiments. J Biomol NMR 13, 223–232 (1999). https://doi.org/10.1023/A:1008301324954
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DOI: https://doi.org/10.1023/A:1008301324954