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- W2145665280 endingPage "1562" @default.
- W2145665280 startingPage "1543" @default.
- W2145665280 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." @default.
- W2145665280 created "2016-06-24" @default.
- W2145665280 creator A5062485923 @default.
- W2145665280 date "1992-12-01" @default.
- W2145665280 modified "2023-09-29" @default.
- W2145665280 title "Internal water molecules and H-bonding in biological macromolecules: A review of structural features with functional implications" @default.
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