INTERNAL WATER-MOLECULES AND H-BONDING IN BIOLOGICAL MACROMOLECULES - A REVIEW OF STRUCTURAL FEATURES WITH FUNCTIONAL IMPLICATIONS

Conserved structural patterns of internal water molecules and/or H-bond chains were observed and are here correlated in this review, which then describes two functional properties: equilibration of hydrostatic pressure and proton transport. Available evidence in support of these hypotheses is presented, together with suggested experiments to test them. High-resolution crystal structures of a variety of proteins were studied with interactive computer graphics. Conserved H-bonding linkages may be used as a paradigm for a rationalization of proton transport in membranes. The concept of the ''proton wire,'' which links buried active-site amino acids with the surface of the protein raises the more general question of the functional role of the various molecular components