AI Article Synopsis
- The study explores how buffer-specific conditions at pH 7.15 affect the molecular motion of BSA (bovine serum albumin) and lysozyme by altering the protein surface charge and protein-protein interactions.
- Researchers used dynamic light scattering and nuclear magnetic resonance to calculate interaction parameters based on diffusion coefficients across different protein concentrations.
- Findings challenge the traditional use of the Henderson-Hasselbalch equation, which has long been relied upon for understanding pH buffers in various scientific fields.
Article Abstract
BSA and lysozyme molecular motion at pH 7.15 is buffer-specific. Adsorption of buffer ions on protein surfaces modulates the protein surface charge and thus protein-protein interactions. Interactions were estimated by means of the interaction parameter obtained from plots of diffusion coefficients at different protein concentrations ( = [1 + ]) via dynamic light scattering and nuclear magnetic resonance. The obtained results agree with recent findings confirming doubts regarding the validity of the Henderson-Hasselbalch equation, which has traditionally provided a basis for understanding pH buffers of primary importance in solution chemistry, electrochemistry, and biochemistry.
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| http://dx.doi.org/10.1021/acs.jpclett.0c01900 | DOI Listing |
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