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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 concentratio...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9350988/ https://www.ncbi.nlm.nih.gov/pubmed/35837993 http://dx.doi.org/10.1039/d2cc02360a |
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author | Ackermann, Katrin Wort, Joshua L. Bode, Bela E. |
author_facet | Ackermann, Katrin Wort, Joshua L. Bode, Bela E. |
author_sort | Ackermann, Katrin |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-9350988 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | The Royal Society of Chemistry |
record_format | MEDLINE/PubMed |
spelling | pubmed-93509882022-08-29 Pulse dipolar EPR for determining nanomolar binding affinities Ackermann, Katrin Wort, Joshua L. Bode, Bela E. Chem Commun (Camb) Chemistry 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. The Royal Society of Chemistry 2022-07-11 /pmc/articles/PMC9350988/ /pubmed/35837993 http://dx.doi.org/10.1039/d2cc02360a Text en This journal is © The Royal Society of Chemistry https://creativecommons.org/licenses/by/3.0/ |
spellingShingle | Chemistry Ackermann, Katrin Wort, Joshua L. Bode, Bela E. Pulse dipolar EPR for determining nanomolar binding affinities |
title | Pulse dipolar EPR for determining nanomolar binding affinities |
title_full | Pulse dipolar EPR for determining nanomolar binding affinities |
title_fullStr | Pulse dipolar EPR for determining nanomolar binding affinities |
title_full_unstemmed | Pulse dipolar EPR for determining nanomolar binding affinities |
title_short | Pulse dipolar EPR for determining nanomolar binding affinities |
title_sort | pulse dipolar epr for determining nanomolar binding affinities |
topic | Chemistry |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9350988/ https://www.ncbi.nlm.nih.gov/pubmed/35837993 http://dx.doi.org/10.1039/d2cc02360a |
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