Pulse dipolar EPR for determining nanomolar binding affinities
MetadataShow full item record
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.
Ackermann , K , Wort , J & Bode , B E 2022 , ' Pulse dipolar EPR for determining nanomolar binding affinities ' , Chemical Communications , vol. 58 , no. 63 , pp. 8790-8793 . https://doi.org/10.1039/D2CC02360A
Copyright © 2022 The Author(s). This article is licensed under a Creative Commons Attribution 3.0 Unported Licence.
DescriptionThis research was funded, in whole or in part, by the Wellcome Trust (204821/Z/16/Z). BEB and KA acknowledge support by the Leverhulme Trust (RPG-2018–397). JLW acknowledges support by the BBSRC DTP Eastbio. BEB acknowledges equipment funding by BBSRC (BB/R013780/1 and BB/T017740/1).
Items in the St Andrews Research Repository are protected by copyright, with all rights reserved, unless otherwise indicated.