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. 1992 Dec;1(12):1543–1562. doi: 10.1002/pro.5560011203

Internal water molecules and H-bonding in biological macromolecules: a review of structural features with functional implications.

E Meyer 1
PMCID: PMC2142137  PMID: 1304887

Abstract

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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Selected References

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