Internal Water Molecules and H-bonding in Biological Macromolecules: A Review of Structural Features with Functional Implications

Biographics Laboratory, Dept. of Biochemistry and Biophysics, Texas A&M University, College Station, Texas USA 77843-2128 Phone: (409) 845-1744 FAX: (409) 845-9274

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.

"Internal Water Molecules and H-bonding in Biological Macromolecules: A Review of Structural Features with Functional Implications." E. Meyer (1992). Protein Science 1:1543-1562.

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