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Pulse dipolar EPR for determining nanomolar binding affinities.

ABSTRACT: Protein interaction studies often require very low concentrations and highly sensitive biophysical methods. Here, we demonstrate that pulse dipolar electron paramagnetic resonance spectroscopy allows measuring dissociation constants in the nanomolar range. This approach is appealing for concentration-limited biomolecular systems and medium-to-high-affinity binding studies, demonstrated here at 50 nanomolar protein concentration.

SUBMITTER: Ackermann K

PROVIDER: S-EPMC9350988 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature

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Pulse dipolar EPR for determining nanomolar binding affinities.

Ackermann Katrin K Wort Joshua L JL Bode Bela E BE

Chemical communications (Cambridge, England) 20220804 63

Protein interaction studies often require very low concentrations and highly sensitive biophysical methods. Here, we demonstrate that pulse dipolar electron paramagnetic resonance spectroscopy allows measuring dissociation constants in the nanomolar range. This approach is appealing for concentration-limited biomolecular systems and medium-to-high-affinity binding studies, demonstrated here at 50 nanomolar protein concentration. ...[more]

PMID: 35837993

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