What is it about?

Using unique nuclear magnetic resonance (NMR) approaches, the weak anion-protein interactions were quantified and visualized. The release of the anions from the protein surface upon formation of a protein–DNA complex was also observed. The experimental data were compared with predictions from the Poisson-Boltzmann theory.

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Why is it important?

Living systems require ions in cellular fluids. These ions electrostatically interact with biological macromolecules and influence their functions. Because ion-protein interactions are generally weak and ions dynamically change their locations with respect to proteins, investigations of ion-protein interactions are challenging. This experimental study presents unique insight into how anions behave around proteins.


I hope that the experimental and theoretical biophysical research communities find this work helpful to understand how anions behave around proteins.

Junji Iwahara
University of Texas Medical Branch

Read the Original

This page is a summary of: Quantifying and visualizing weak interactions between anions and proteins, Proceedings of the National Academy of Sciences, December 2020, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2015879118.
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