FEMS Immunology & Medical Microbiology · 2009 · 24 citations · 34 references
Life SciencesBiochemistryMolecular BiologyProtein BiochemistryProtein Structure PredictionProteomicsMembrane Protein TopologyMembrane ProteinsProtein CharacterizationProtein Sequence AnalysisProtein StructureProteolytic ProcessingMembrane Protein IdentificationMembrane Protein MotifsMembrane Protein Topology AnalysisOuter Membrane PorinsOuter Membrane ProteinsPorin ProteinsProtease Cleavage SitesProteolytic Digestion Analysis
The protein composition and N-terminal sequences of proteins in the outer membrane of Chlamydia trachomatis L2 were analysed following isolation of N-terminal peptides using combined fractional diagonal chromatography and identification by liquid chromatography tandem MS. Acetylation of primary amino groups of in vivo generated proteolytic cleavage sites facilitated identification of such sites in known outer membrane proteins (MOMPs). Our results further support a proposed prediction of the topology of the MOMPs. Furthermore, a previously unknown MOMP, CTL0626 (Ct372), was assigned as an MOMP with a carbohydrate-selective porin (OprB) family motif, and the presence of CTL0626 was confirmed using antibodies raised against the protein.
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Improved Prediction of Signal Peptides: SignalP 3.0
Jannick Dyrløv Bendtsen, Henrik Nielsen, Gunnar von Heijne et al. · Journal of Molecular Biology · 2004 · 6.4K citations