Logo image
Specific buffer effects on the intermolecular interactions among protein molecules at physiological pH
Journal article   Peer reviewed

Specific buffer effects on the intermolecular interactions among protein molecules at physiological pH

A. Salis, L. Cappai, C. Carucci, D.F. Parsons and M. Monduzzi
The Journal of Physical Chemistry Letters, Vol.11(16), pp.6805-6811
2020
url
Link to Published Version *Subscription may be requiredView

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 kD obtained from plots of diffusion coefficients at different protein concentrations (Dapp = D0[1 + kDCprotein]) 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.

Details

UN Sustainable Development Goals (SDGs)

This output has contributed to the advancement of the following goals:

#6 Clean Water and Sanitation

Source: InCites

Metrics

InCites Highlights

These are selected metrics from InCites Benchmarking & Analytics tool, related to this output

Collaboration types
Domestic collaboration
International collaboration
Citation topics
2 Chemistry
2.89 Ionic, Molecular & Complex Liquids
2.89.677 Liquid Water
Web Of Science research areas
Chemistry, Physical
Materials Science, Multidisciplinary
Nanoscience & Nanotechnology
Physics, Atomic, Molecular & Chemical
ESI research areas
Chemistry
Logo image