I have come across some literature regarding Protein-ion interactions. In some of them, the direct mechanism is explained (i.e charge based neutralization, effect of charge density etc.) and in some of them, the indirect mechanism is explained (i.e. through solvation/hydration layer and preferential exclusion etc.)
I want to know which mechanism is right? or is it that both of them happen but at different ionic concentrations?
If someone can please spare some time to explain this, I would be obliged.
Both of them happen for different proteins. For example, a metallic protease might directly interact with the metal in its center using complex bonding. Or alternatively, an sodium channel might acquire its selectivity by sensing sodium's unique hydration shell. The chemical possibilities are near-endless..
Hi John, Thanks for the answer. But, my question is more in the sense of "aggregation of proteins due to ions". Like what is the actual mechanism of aggregation? Is it due to direct interaction of protein and ions or is it through ion interacting with solvation & hydration layer around protein?
Hi Rahul, apparently I am searching for the answer of the same question too. (Just) I think protein might not easily aggragate because of direct interactions with the ions
- Badges
- Science topic
- Similar topics
- Chemistry
- Biochemistry