Abstract
Abstract The (ν2 + ν3) combination band of water has been investigated in aqueous solutions of proline, glycinebetaine and glycerol and in a three component solution with each of these substances and albumin. It is shown that the hydrogen bonding strength between the water protons and proline or betaine is higher than between water and glycerol. Betaine exhibits a higher affinity versus the oxygen of water than does proline. The water binding capacity of pure proline solutions is unchanged in a three-component solution with albumin. Proline neither enhances nor reduces the solubility of this highly soluble protein. In contrast, in a three-component solution with betaine, the solubility of both betaine and album in is reduced. It is assumed that these solute particles compete for the same binding position on the water molecule. Concentrated glycerol solutions with very low water concentrations dissolve a considerable amount of albumin, which points to the fact that the protein must be partly dissolved in glycerol itself.
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