Results 11 to 20 of about 268,169 (218)
Extraction and Electrophoretic Analysis of Bacterial Lipopolysaccharides and Outer Membrane Proteins
Lipopolysaccharides (LPS) (or lipooligosaccharides [LOS], which lack the O-antigen side chains characteristic of LPS), and outer membrane proteins (OMP) are major cell-surface molecules in the outer membrane (OM) of gram-negative bacteria.
Yue Lee, Thomas Inzana
doaj +3 more sources
Mechanisms of Protein Export across the Bacterial Outer Membrane [PDF]
Gram-negative bacteria secrete a wide range of proteins whose functions include biogenesis of organelles, such as pili and flagella; nutrient acquisition; virulence; and efflux of drugs and other toxins. Export of these proteins to the bacterial surface involves transport across the inner membrane (IM), periplasm, and outer membrane (OM) of the cell ...
Maria Kostakioti +3 more
openalex +5 more sources
Structure and function of bacterial outer membrane proteins: barrels in a nutshell [PDF]
The outer membrane protects Gram‐negative bacteria against a harsh environment. At the same time, the embedded proteins fulfil a number of tasks that are crucial to the bacterial cell, such as solute and protein translocation, as well as signal transduction.
Ralf Koebnik +2 more
openalex +4 more sources
Protein oligomerization in the bacterial outer membrane (Review) [PDF]
The formation of homo-oligomeric assemblies is a well-established characteristic of many soluble proteins and enzymes. Oligomerization has been shown to increase protein stability, allow allosteric cooperativity, shape reaction compartments and provide multivalent interaction sites in soluble proteins. In comparison, our understanding of the prevalence
Guoyu Meng +4 more
openalex +4 more sources
The Assembly of Beta-Barrel Proteins into Bacterial Outer Membranes [PDF]
In order to cause disease, bacterial pathogens must (i) avoid immune detection, (ii) inhibit immune responses, and (iii) induce pathology favoring bacterial replication. In gram-negative bacteria, pathogenesis depend on structures assembled in the bacterial outer membrane.
Trevor Lithgow
openalex +3 more sources
The structure of bacterial outer membrane proteins
Integral membrane proteins come in two types, alpha-helical and beta-barrel proteins. In both types, all hydrogen bonding donors and acceptors of the polypeptide backbone are completely compensated and buried while nonpolar side chains point to the membrane. The alpha-helical type is more abundant and occurs in cytoplasmic (or inner) membranes, whereas
Georg E. Schulz
openalex +5 more sources
Selectivity in Lipid Binding to the Bacterial Outer Membrane Protein OmpF [PDF]
The outer membrane porin OmpF from Escherichia coli has been reconstituted into lipid bilayers of defined composition, and fluorescence spectroscopy is used to characterize its interaction with the surrounding lipid. OmpF is a trimer within the membrane.
Aisling H. O’Keeffe +2 more
openalex +6 more sources
Insertion of proteins and lipopolysaccharide into the bacterial outer membrane [PDF]
The bacterial outer membrane contains phospholipids in the inner leaflet and lipopolysaccharide (LPS) in the outer leaflet. Both proteins and LPS must be frequently inserted into the outer membrane to preserve its integrity. The protein complex that inserts LPS into the outer membrane is called LptDE, and consists of an integral membrane protein, LptD,
Istvan Botos +2 more
openalex +3 more sources
Interactions between folding factors and bacterial outer membrane proteins [PDF]
SummaryThe outer membrane is the first line of contact between Gram‐negative bacteria and their external environment. Embedded in the outer membrane are integral outer membrane proteins (OMPs) that perform a diverse range of tasks. OMPs are synthesized in the cytoplasm and are translocated across the inner membrane and probably diffuse through the ...
Jesper E. Mogensen, Daniel E. Otzen
openalex +5 more sources
The Ton complex is a molecular motor at the inner membrane of Gram-negative bacteria that uses a proton gradient to apply forces on outer membrane (OM) proteins to permit active transport of nutrients into the periplasmic space.
Anna C. Ratliff +2 more
doaj +1 more source

