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PMID: 1304887 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Review

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

Protein science : a publication of the Protein Society ·Vol. 1 ·No. 12 ·1992-12-00 ·Pages 1543-62

Meyer E

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.

MeSH Terms
Amino Acid Sequence Binding Sites Endopeptidases/chemistry,metabolism Enzymes/chemistry,metabolism Hydrogen Bonding Membrane Proteins/chemistry,metabolism Models, Molecular Protein Conformation Protein Structure, Secondary Proteins/chemistry,metabolism Water/metabolism
Chemicals
Enzymes Membrane Proteins Proteins Water Endopeptidases
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Meyer E
Department of Biochemistry and Biophysics, Texas A&M University, College Station 77843-2128.
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Article Info
Journal
Protein science : a publication of the Protein Society
Abbr.
Protein Sci
ISSN
0961-8368
DOI
10.1002/pro.5560011203
Published
1992-12-00
Pages
1543-62
Language
English
Region
United States
NLM ID
9211750
PMCID
PMC2142137
Subset
IM
External Links
PubMed source DOI: 10.1002/pro.5560011203 PMC Full Text View journal details
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