Protein Science, Vol 1, Issue 12 1543-1562, Copyright © 1992 by Cold Spring Harbor Laboratory Press

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Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications(1)

E. MEYER
Biographics Laboratory, Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas 77843-2128

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
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