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.
Meyer
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Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843-2128.
D000595:Amino Acid Sequence; D001665:Binding Sites; D010450:Endopeptidases / Q000737:chemistry / Q000378:metabolism; D004798:Enzymes / Q000737:chemistry* / Q000378:metabolism; D006860:Hydrogen Bonding; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D014867:Water / Q000378:metabolism*
D004798:Enzymes; D008565:Membrane Proteins; D011506:Proteins; D014867:Water; D010450:Endopeptidases