In all biologically relevant media, proteins interact in the presence of surrounding ions, and such interactions are water-mediated. Water molecules play a crucial role in the restructuring of proteins in solution and indeed in their biological activity. Surface water dynamics and proton exchange at protein surfaces is investigated here using NMR relaxometry, for two well-known globular proteins, lysozyme and bovine serum albumin, with particular attention to the role of surface ions. We present a unified model of surface water dynamics and proton exchange, accounting simultaneously for the observed longitudinal and transverse relaxation rates. The most notable effect of salt (0.1 M) concerns the slow surface water dynamics, related to rare water molecules embedded in energy wells on the protein surface. This response is protein-specific. On the other hand, the proton exchange time between labile protein-protons and water-protons at the protein surface seems to be very similar for the two proteins and is insensitive to the addition of salts at the concentration studied.
Keywords: NMR relaxometry; Protein; Proton exchange; Surface; Water dynamics.