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.
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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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