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Measurement of Ligand-Target Residence Times by ¹H Relaxation Dispersion NMR Spectroscopy.

ABSTRACT: A ligand-observed ¹H NMR relaxation experiment is introduced for measuring the binding kinetics of low-molecular-weight compounds to their biomolecular targets. We show that this approach, which does not require any isotope labeling, is applicable to ligand-target systems involving proteins and nucleic acids of variable molecular size. The experiment is particularly useful for the systematic investigation of low affinity molecules with residence times in the micro- to millisecond time regime.

SUBMITTER: Moschen T

PROVIDER: S-EPMC5150660 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature

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Measurement of Ligand-Target Residence Times by 1H Relaxation Dispersion NMR Spectroscopy.

Moschen Thomas T Grutsch Sarina S Juen Michael A MA Wunderlich Christoph H CH Kreutz Christoph C Tollinger Martin M

Journal of medicinal chemistry 20161129 23

A ligand-observed 1H NMR relaxation experiment is introduced for measuring the binding kinetics of low-molecular-weight compounds to their biomolecular targets. We show that this approach, which does not require any isotope labeling, is applicable to ligand-target systems involving proteins and nucleic acids of variable molecular size. The experiment is particularly useful for the systematic investigation of low affinity molecules with residence times in the micro- to millisecond time ...[more]

PMID: 27933946

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