Abstract
Changes in background salt and buffer are known to influence the properties of proteins. The reasons have remained obscure. The challenge posed by many such problems is this. Can physical chemistry contribute any predictive quantitative insights to what is in effect the simplest macromolecular solution behavior? Or must all remain specific? Our thesis is that it can. For definiteness we consider ...
Abstract
Changes in background salt and buffer are known to influence the properties of proteins. The reasons have remained obscure. The challenge posed by many such problems is this. Can physical chemistry contribute any predictive quantitative insights to what is in effect the simplest macromolecular solution behavior? Or must all remain specific? Our thesis is that it can. For definiteness we consider here as an illustrative example: surface pH and protonation equilibria of cytochrome c. We demonstrate an important role for ionic dispersion forces, missing from previous theoretical treatments. Unlike charge interactions these are different for each ionic species, and act between a protein and both salt and buffer ions. The charge of proteins depends not only on pH, ionic charge, and salt concentration. Taking ionic dispersion forces into account goes some way towards explaining the dependence on ionic species. We demonstrate why the addition of buffer can have profound effects, including reversal of the salt dependence of the protein charge.
Altmetric