Results 51 to 60 of about 273,841 (296)
Selectivity in Lipid Binding to the Bacterial Outer Membrane Protein OmpF [PDF]
Biophysical Journal, 2000 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.
O'Keeffe, Aisling H. +2 more
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Frontiers in Microbiology, 2021 Antibiotic–adjuvant combinatory therapy serves as a viable treatment option in addressing antibiotic resistance in the clinical setting. This study was carried out to assess and characterize the adjuvant potential and mode of action of linalool against ...
Shun-Kai Yang +7 more
doaj +1 more source
Structure and function of bacterial dynamin-like proteins [PDF]
, 2012 Membrane dynamics are essential for numerous cellular processes in eukaryotic and prokaryotic cells. In eukaryotic cells, membrane fusion and fission are often catalyzed by large GTPases of the dynamin protein family. These proteins couple GTP hydrolysis
Bramkamp, Marc
core +1 more source
Journal of Pharmaceutical Analysis, 2021 Mining of plant-derived antimicrobials is the major focus at current to counter antibiotic resistance. This study was conducted to characterize the antimicrobial activity and mode of action of linalyl anthranilate (LNA) against carbapenemase-producing ...
Shun-Kai Yang +5 more
doaj +1 more source
Imaging and 3D reconstruction of membrane protein complexes by cryo-electron microscopy and single particle analysis [PDF]
, 2006 Cryo-electron microscopy (cryo-EM) in combination with single particle image processing and volume reconstruction is a powerful technology to obtain medium-resolution structures of large protein complexes, which are extremely difficult to crystallize and ...
Gregorini, Marco
core +1 more source
Folding of a bacterial integral outer membrane protein is initiated in the periplasm [PDF]
Nature Communications, 2017 AbstractThe Bam complex promotes the insertion of β-barrel proteins into the bacterial outer membrane, but it is unclear whether it threads β-strands into the lipid bilayer in a stepwise fashion or catalyzes the insertion of pre-folded substrates.
Rakesh Sikdar +3 more
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Construction of a bacterial surface display system based on outer membrane protein F
Microbial Cell Factories, 2019 Background Bacterial surface display systems were developed to surface expose heterologous proteins or peptides for different applications, such as peptide libraries screening and live bacterial vaccine design.
Tingting Chen +12 more
doaj +1 more source
, 1990 The cytochrome c import pathway differs markedly from the general route taken by the majority of other imported proteins, which is characterized by the import involvement of namely, surface receptors, the general insertion protein (GIP), contact sites ...
Berkout +68 more
core +1 more source
The structure of bacterial outer membrane proteins
Biochimica et Biophysica Acta (BBA) - Biomembranes, 2002 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
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Assembly of β-barrel proteins into bacterial outer membranes
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2014 Membrane proteins with a β-barrel topology are found in the outer membranes of Gram-negative bacteria and in the plastids and mitochondria of eukaryotic cells. The assembly of these membrane proteins depends on a protein folding reaction (to create the barrel) and an insertion reaction (to integrate the barrel within the outer membrane).
Selkrig, Joel +3 more
openaire +3 more sources