Results 31 to 40 of about 3,838,185 (278)

Dissecting Escherichia coli outer membrane biogenesis using differential proteomics. [PDF]

open access: yesPLoS ONE, 2014
The cell envelope of Gram-negative bacteria is a complex multi-layered structure comprising an inner cytoplasmic membrane and an additional asymmetric lipid bilayer, the outer membrane, which functions as a selective permeability barrier and is essential
Alessandra M Martorana   +7 more
doaj   +1 more source

Stress-Responsive Periplasmic Chaperones in Bacteria

open access: yesFrontiers in Molecular Biosciences, 2021
Periplasmic proteins are involved in a wide range of bacterial functions, including motility, biofilm formation, sensing environmental cues, and small-molecule transport. In addition, a wide range of outer membrane proteins and proteins that are secreted
Hyunhee Kim   +4 more
doaj   +1 more source

Characterization of Translocation Contact Sites Involved in the Import of Mitochondrial Proteins [PDF]

open access: yes, 1987
Import of proteins into the mitochondrial matrix requires translocation across two membranes. Translocational intermediates of mitochondrial proteins, which span the outer and inner membrane simultaneously and thus suggest that translocation occurs in ...
Herzog, Volker   +5 more
core   +2 more sources

Preparation of Bacterial Outer Membrane Vesicles for Characterisation of Periplasmic Proteins in Their Native Environment

open access: yesBio-Protocol, 2020
Bacterial outer membrane vesicles (OMVs) are naturally formed by budding from the outer membrane of Gram-negative bacteria. OMVs consist of a lipid bilayer identical in composition to the original outer membrane and contain periplasmic content within ...
Johannes Thoma, Björn Burmann
doaj   +1 more source

β-Barrel Assembly Machinery (BAM) Complex as Novel Antibacterial Drug Target

open access: yesMolecules, 2023
The outer membrane of Gram-negative bacteria is closely related to the pathogenicity and drug resistance of bacteria. Outer membrane proteins (OMPs) are a class of proteins with important biological functions on the outer membrane.
Qian Xu, Min Guo, Feiyuan Yu
doaj   +1 more source

Effect of Energy Metabolism on Protein Motility in the Bacterial Outer Membrane [PDF]

open access: yesBiophysical Journal, 2009
We demonstrate the energy dependence of the motion of a porin, the lambda-receptor, in the outer membrane of living Escherichia coli by single molecule investigations. By poisoning the bacteria with arsenate and azide, the bacterial energy metabolism was stopped.
Ryder, Tabita Winther   +4 more
openaire   +3 more sources

Prediction of β-barrel membrane proteins by searching for restricted domains [PDF]

open access: yes, 2005
BACKGROUND: The identification of beta-barrel membrane proteins out of a genomic/proteomic background is one of the rapidly developing fields in bioinformatics. Our main goal is the prediction of such proteins in genome/proteome wide analyses.
Mirus, O.   +5 more
core   +1 more source

Interactions between folding factors and bacterial outer membrane proteins [PDF]

open access: yesMolecular Microbiology, 2005
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 ...
Mogensen, Jesper E., Otzen, Daniel E.
openaire   +3 more sources

Membrane proteins in the outer mebrane of plastids and mitochondria [PDF]

open access: yes, 2006
Channels of the plastid and mitochondrial outer membranes facilitate the turnover of molecules and ions via these membranes. Although channels have been studied many questions pertaining to the whole diversity of plastid and mitochondrial channels in ...
Ilkavets, Iryna
core   +1 more source

The structure of bacterial outer membrane proteins

open access: yesBiochimica 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
openaire   +3 more sources

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