The outer membrane proteins (OMPs) from Gram-negative bacteria form a disti
nct group of integral membrane proteins with unusual primary, secondary and
tertiary structures. Unlike typical prokaryotic or eukaryotic membrane pro
teins, bacterial OMPs contain primarily polar sequences, arranged in amphip
athic antiparallel beta-barrels, and inclined to the plane of the membrane.
Due to their unique structure, OMPs have recently become the subject of ex
tensive study. This article reviews (i) experimental and theoretical approa
ches of topological analysis used in the study of OMPs, and (ii) the applic
ations of OMPs.