Dehydrons Are Loosely Hydrated

By contrast, exposed hydrophobic residues like Val35 may be effectively clathrated or accommodated within a water cavity that introduces a minimal perturbation of the tetrahedral hydrogen bonding network of water. In fact, clathration actually tightens the hydration shell (Figs. 4.1b and 4.2). 

4 Wrapping Deficiencies and De-wetting Patterns in Soluble Proteins 

To compute the de-wetting of intramolecular hydrogen bonds, we take into account the modulation of local permittivity determined by a change in the environmental coordinates Rjjy=1 K Ry, R y—j A where R is the position 

The time averages of the magnitude and variance of the de-wetting field were computed for each residue in the protein (Fig. 4.3). 

Comparison of Figs. 4.1b and 4.3 prompt the following conclusions (a) the tightness of the hydration shell of a soluble protein is not uniform, yielding an uneven distribution of mobilities for hydrating molecules (b) dehydrons generate the most pronounced loosening of the hydration shell and (c) dehydrons are endowed with dehydration propensities. 

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