Desolvation shell of hydrogen bonds in folded proteins, protein complexes and folding pathways.

A few backbone hydrogen bonds (HBS) in native protein folds are poorly protected from water attack: their desolvation shell contains an inordinately low number of hydrophobic residues. Thus, an approach by solvent-structuring moieties of a binding partner should contribute significantly to enhance their stability. This effect represents an important factor in the site specificity inherent to protein binding, as inferred from a strong correlation between poorly desolvated HBs and binding sites. The desolvation shells were also examined in a dynamic context: except for a few singular under-protected bonds, the size of desolvation shells is preserved along the folding trajectory.