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The determination of a β-barrel membrane protein structure by NMR spectroscopy is an important accomplishment in structural biology. This study provided critical information about the dynamics of the β-barrel motions in the bilayer, and showed that the barrel is most rigid in the bilayer center and most flexible near the bilayer interfaces.
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This paper describes one of several algorithms developed recently to identify β-barrel membrane proteins. Taken together, these algorithms have established that the OM β-barrel proteome of Gram-negative bacteria encompasses about 2-3% of the genome.
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Wimley W.C. Toward genomic identification of β-barrel membrane proteins: composition and architecture of known structures. Protein Sci. 11:2002;301-312 This paper describes one of several algorithms developed recently to identify β-barrel membrane proteins. Taken together, these algorithms have established that the OM β-barrel proteome of Gram-negative bacteria encompasses about 2-3% of the genome.
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A very nice biophysical study of pore formation in the protein perfringolysin. Multiple independent techniques were used to show that two separate segments of the protein each contribute to the multimeric pore. The same techniques demonstrated that these segments span a bilayer membrane as β-hairpins.
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This paper describes one of several algorithms developed recently to identify β-barrel membrane proteins. Taken together, these algorithms have established that the OM β-barrel proteome of Gram-negative bacteria encompasses about 2-3% of the genome.
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Zhai Y., Saier M.H. Jr. The β-barrel finder (BBF) program, allowing identification of outer membrane β-barrel proteins encoded within prokaryotic genomes. Protein Sci. 11:2002;2196-2207 This paper describes one of several algorithms developed recently to identify β-barrel membrane proteins. Taken together, these algorithms have established that the OM β-barrel proteome of Gram-negative bacteria encompasses about 2-3% of the genome.
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This paper describes one of several algorithms developed recently to identify β-barrel membrane proteins. Taken together, these algorithms have established that the OM β-barrel proteome of Gram-negative bacteria encompasses about 2-3% of the genome.
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Analysis of the outer membrane proteome of Caulobacter crescentus by two-dimensional electrophoresis and mass spectrometry
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Phadke N.D., Molloy M.P., Steinhoff S.A., Ulintz P.J., Andrews P.C., Maddock J.R. Analysis of the outer membrane proteome of Caulobacter crescentus by two-dimensional electrophoresis and mass spectrometry. Proteomics. 1:2001;705-720.
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Profiling the alkaline membrane proteome of Caulobacter crescentus with two-dimensional electrophoresis and mass spectrometry
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Technical proteomics work that is beginning to reveal the true complexity of the OMs of Gram-negative bacteria. This work, taken together with [19], has shown that the OM of this Gram-negative bacterium contains many β-barrels of unknown function.
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Molloy M.P., Phadke N.D., Chen H., Tyldesley R., Garfin D.E., Maddock J.R., Andrews P.C. Profiling the alkaline membrane proteome of Caulobacter crescentus with two-dimensional electrophoresis and mass spectrometry. Proteomics. 2:2002;899-910 Technical proteomics work that is beginning to reveal the true complexity of the OMs of Gram-negative bacteria. This work, taken together with [19], has shown that the OM of this Gram-negative bacterium contains many β-barrels of unknown function.
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Proteomics
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This paper contains a wealth of information about the genomics, phylogenetics and distributions of the major families of OM β-barrel protein transporters. The protein families covered are the OM factor proteins, the OM ushers, secretins, autotransporters and two-partner secretion pores.
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Yen M.R., Peabody C.R., Partovi S.M., Zhai Y., Tseng Y.H., Saier M.H. Protein-translocating outer membrane porins of Gram-negative bacteria. Biochim. Biophys. Acta. 1562:2002;6-31 This paper contains a wealth of information about the genomics, phylogenetics and distributions of the major families of OM β-barrel protein transporters. The protein families covered are the OM factor proteins, the OM ushers, secretins, autotransporters and two-partner secretion pores.
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This paper describes the formation of the mitochondrial translocase pore and how pore formation is modulated by some of the other members of the TOM complex. This paper nicely illustrates the interplay between the β-barrel pore protein Tom40 and its associated α-helical membrane protein partners.
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Model K., Prinz T., Ruiz T., Radermacher M., Krimmer T., Kuhlbrandt W., Pfanner N., Meisinger C. Protein translocase of the outer mitochondrial membrane: role of import receptors in the structural organization of the TOM complex. J. Mol. Biol. 316:2002;657-666 This paper describes the formation of the mitochondrial translocase pore and how pore formation is modulated by some of the other members of the TOM complex. This paper nicely illustrates the interplay between the β-barrel pore protein Tom40 and its associated α-helical membrane protein partners.
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