Literature DB >> 10661467

Bacterial outer membrane proteins: topological analyses and biotechnological perspectives.

C Stathopoulos1.   

Abstract

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.

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Year:  1999        PMID: 10661467

Source DB:  PubMed          Journal:  Membr Cell Biol        ISSN: 1023-6597


  2 in total

1.  Sequence polymorphism, predicted secondary structures, and surface-exposed conformational epitopes of Campylobacter major outer membrane protein.

Authors:  Q Zhang; J C Meitzler; S Huang; T Morishita
Journal:  Infect Immun       Date:  2000-10       Impact factor: 3.441

2.  Structure-function relationships of the outer membrane translocon Wza investigated by cryo-electron microscopy and mutagenesis.

Authors:  Robert C Ford; Anne L Brunkan-LaMontagne; Richard F Collins; Bradley R Clarke; Robert Harris; James H Naismith; Chris Whitfield
Journal:  J Struct Biol       Date:  2009-02-21       Impact factor: 2.867

  2 in total

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