The specific short-range interactions of a metal cation in water arise from reorientation of the first shell water molecules.
We use a molecular model based on atomistic simulations called 2-shell water coordination number to predict the oxidation rates for several model proteins and therapeutic candidates.
We describe the behavior of the local molecular structure under increasing temperatures and the effect of peptide interactions with nearest hydration shell water molecules on peptide mobility and propensity to exhibit structural transitions.
Moreover, to enter the channel, the G0-G4 PAMAM dendrimers are expected to reorganize their solvation structure, losing all or almost all shell water molecules and counterions.
In general, however, these results indicate that intracellular solvent viscosity displays the same features as viscosity in aqueous protein solutions at the nm scale: unperturbed properties of bulk water, with increased solvent viscosity and reduced dynamics of hydration shell water.
The three hydrophilic residues Glu98, Arg80 and Tyr70, which form a hydrophilic gate to the active site cavity and coordinate an outer shell water molecule (see Fig. 13), are crucial for efficient O2 reduction.
And their shell water supply has a specific balance of iron.
