Bacterial outer membrane proteins: topological analyses and biotechnological perspectives.
The outer membrane proteins (OMPs) from gram-negative bacteria form a distinct group of integral membrane proteins with unusual primary, secondary and tertiary structures. Unlike typical prokaryotic and eukaryotic membrane proteins, bacterial OMPs contain primarily polar sequences, arranged in amphipathic antiparallel beta-barrels, and inclined to the plane of the membrane. Due to their unique structure, OMPs have recently become the subject of extensive study. This article reviews (i) experimental and theoretical approaches of topological analyses used in the study of OMPs, and (ii) the applications of OMPs.
Stathopoulos
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Washington University, Department of Biology, St. Louis, MO 63130, USA. cstatho@biodec.wustl.edu
D000595:Amino Acid Sequence; D000818:Animals; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D001709:Biotechnology; D005544:Forecasting; D006801:Humans; D008969:Molecular Sequence Data; D018272:Porins / Q000737:chemistry; D011487:Protein Conformation; D011993:Recombinant Fusion Proteins / Q000737:chemistry / Q000235:genetics / Q000276:immunology
D001425:Bacterial Outer Membrane Proteins; D018272:Porins; D011993:Recombinant Fusion Proteins