Pulse dipolar EPR for determining nanomolar binding affinities

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.

Automated summary

Pulse dipolar electron paramagnetic resonance spectroscopy allows measurement of dissociation constants in the nanomolar range, making it suitable for concentration-limited biomolecular systems and medium-to-high-affinity binding studies.