Characterization of the Major Envelope Protein from Escherichia coli REGULAR ARRANGEMENT ON THE PEPTIDOGLYCAN AND UNUSUAL DODECYL SULFATE BINDING
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TLDR
The major envelope protein from Escherichia coli has been purified by differential heat extraction in dodecyl sulfate and subsequently freed of the detergent, and its molecular weight agrees with that derived from the mobility of the major band observed in standard dodecYL sulfate gel electrophoretic analysis of unfractionated cell envelopes after treatment at 100°.About:
This article is published in Journal of Biological Chemistry.The article was published on 1974-12-25 and is currently open access. It has received 711 citations till now. The article focuses on the topics: Sodium dodecyl sulfate & Protein quaternary structure.read more
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Molecular Basis of Bacterial Outer Membrane Permeability Revisited
TL;DR: This review summarizes the development in the field since the previous review and begins to understand how this bilayer of the outer membrane can retard the entry of lipophilic compounds, owing to increasing knowledge about the chemistry of lipopolysaccharide from diverse organisms and the way in which lipopoly Saccharide structure is modified by environmental conditions.
Journal ArticleDOI
Molecular basis of bacterial outer membrane permeability.
Hiroshi Nikaido,Martti Vaara +1 more
TL;DR: It is becoming increasingly clear that the outer membrane is very important in the physiology of gram-negative bacteria in making them resistant to host defense factors such as lysozyme, P-lysin, and various leukocyte proteins.
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Analysis of membrane and surface protein sequences with the hydrophobic moment plot.
TL;DR: An algorithm has been developed which identifies alpha-helices involved in the interactions of membrane proteins with lipid bilayers and which distinguishes them from helices in soluble proteins, and suggests four transmembrane helices and a surface-seeking helix in fragment B, the moiety known to have trans Membrane function.
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Crystal structures explain functional properties of two E. coli porins
S. W. Cowan,Tilman Schirmer,Gabriele Rummel,Matthias Steiert,Robin Ghosh,Richard A. Pauptit,Johan N. Jansonius,Jurg P. Rosenbusch +7 more
TL;DR: The crystal structures of matrix porin and phosphoporin both reveal trimers of identical subunits, each subunit consisting of a 16-stranded anti-parallel β-barrel containing a pore.
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Electrophoretic resolution of the ‘major outer membrane protein’ of Escherichia coli K12 into four bands
TL;DR: The cell envelope of Enterobacteriaceae consists of two membranes separated by a peptidoglycan layer, and methods have been developed to separate the cytoplasmic membrane from the outer membrane.
References
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Journal Article
Protein Measurement with the Folin Phenol Reagent
TL;DR: Procedures are described for measuring protein in solution or after precipitation with acids or other agents, and for the determination of as little as 0.2 gamma of protein.
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
Klaus Weber,Mary Osborn +1 more
TL;DR: The results show that the polyacrylamide gel electrophoresis method can be used with great confidence to determine the molecular weights of polypeptide chains for a wide variety of proteins.
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Automatic recording apparatus for use in the chromatography of amino acids.
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Estimation of total, protein-bound, and nonprotein sulfhydryl groups in tissue with Ellman's reagent
Jozef Sedlak,Raymond H. Lindsay +1 more
TL;DR: A simple spectrophotometric method for the routine concomitant determination of sulfhydryl groups in PB- SH, NP-SH, and T-SH fractions in various tissues is reported.