So we're going to have a bunch of positively charged sodium ions and a bunch of negatively charged chloride ions floating around in our aqueous solution. Now, because we don't increase or decrease the amount of water molecules present inside our mixture, what that means is the number of hydrogen bonds that are available to interact with the hydrophilic amino acids of the protein will decrease. And if we decrease the amount of stabilizing hydrogen bonds interacting with our protein, that will destabilize the structure of these individual proteins. And what that means is, if we destabilize the structure of these individual molecules, they will begin to aggregate. And that's because by aggregating, by interacting between the non polar sections of these amino acids, that will in turn, stabilize the structure of this entire aggregate molecule. And so we see that as we add the salt into our mixture, because some of those water molecules that were interacting with the protein before are now forming hydrogen bonds with these ions, dissolved ions, we have less H bonds to basically stabilize the protein.