bacterial membrane

Recent experimental studies show that the initial site of action is the outer bacterial membrane.

This results in a disruption of the structure of the bacterial membrane.

Phosphate-selective porins are a family of outer bacterial membrane proteins.

As they target directly bacterial membranes.

This reaction is coupled to the pumping of four additional protons across the mitochondrial or bacterial membrane.

In addition, it disrupts bacterial membranes by depolarization.

These features mean that it can interact with the anionic lipids in the bacterial membrane, such as phosphatidylglycerol.

Release of signal peptides from bacterial membrane prolipoproteins including murein prolipoprotein.

Because these molecules physically disrupt the bacterial membrane rather than target an intracellular component, bacteria are less able to develop resistance.

The pR contained in the bacterial membranes was shown to act as a light-activated proton pump, but only when retinal is present.

The mechanism of action of other polypeptide antibiotics is thought to be directed to bacterial membranes, but the details are largely unknown.

The bacterial membrane has a different structure from the mammalian plasma membrane, so the protein can only kill pathogenic cells and not human ones.

This enzyme is present in bacterial membranes and in chloroplast thylakoid membranes.

The particles catalyze powerful reactions that break down organic pollutants, volatile organic compounds and bacterial membranes.

One of the primary roles for PE in bacterial membranes is to spread out the negative charge caused by anionic membrane phospholipids.

The C-terminal domain of ActA has a hydrophobic region which anchors the protein in the bacterial membrane.

Unlike eukaryotes, bacterial membranes (with some exceptions e.g. Mycoplasma and methanotrophs) generally do not contain sterols.

This depends on how the agent kills bacteria, either by depleting the bacterial food supply or through bacterial membrane disruption and the kind of monomer used.

The amphipathic N-terminal segment of the alpha- helix is mainly responsible for the increase in permeability of the bacterial membrane which kills the bacteria.

As long as chlorhexidine is incorporated into the bacterial membrane and its substantivity is not impaired, the efficacy of these products should not be affected.

The enzyme is bound to the inner cytoplasmic surface of the bacterial membrane and contains multiple subunits, iron-sulfur centers and a molybdenum cofactor.

However, the hydrophobic interaction is relatively weak when compared to the electrostatic interaction, thus, the antimicrobial peptides will preferentially interact with the bacterial membranes.

Structural similarities to the antimicrobial peptide cecropin A from Hyalophora cecropia suggest that it may function in a similar manner by disrupting the bacterial membrane.

Outer membrane protein W (OmpW) family is a family of evolutionarily related proteins from the outer bacterial membrane.

These include the cytoplasmic side of plasma membranes, the outer leaflet of outer bacterial membranes and mitochondrial membranes.