Department of Chemical and Geological Sciences, University of Cagliari, and Centro NanoBiotecnologie Sardegna (CNBS), Cittadella Universitaria, SS 554 bivio Sestu, 09042 Monserrato (CA), Italy.
Consorzio Interuniversitario per lo Sviluppo dei Sistemi a Grande Interfase (CSGI), Florence, Italy.
J Phys Chem Lett. 2020 Aug 20;11(16):6805-6811. doi: 10.1021/acs.jpclett.0c01900. Epub 2020 Aug 7.
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.
在 pH 值为 7.15 时,BSA 和溶菌酶的分子运动具有缓冲特异性。缓冲离子在蛋白质表面的吸附会调节蛋白质表面电荷,从而影响蛋白质-蛋白质相互作用。通过动态光散射和核磁共振测量不同蛋白质浓度下扩散系数的关系图(= [1 + ]),得到相互作用参数,从而对相互作用进行估计。所得结果与最近的发现一致,这些发现证实了对亨德森-哈塞尔巴尔赫方程有效性的质疑,该方程传统上一直是理解溶液化学、电化学和生物化学中具有重要意义的 pH 缓冲液的基础。