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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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MOMP (Major outer membrane protein) |
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Approximately 40 kDa in size, with five genetically conserved domains and four variable domains that are used to determine the serovar within each species. Characterzed by an N-terminal domain that forms an eight-stranded, anti-parallel β barrel embedded in the outer membrane. The eight strands are connected by four long loops at the outer membrane surface and three short periplasmic turns of the molecule. ... |
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OmcB (Outer membrane complex protein B) |
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A 60-kDa, cysteine-rich protein. All the OmcB proteins of Chlamydiae possess at least one XBBXBX sequence in their N-terminal domains. ... |
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