A multicenter study comparing the bacterial reduction on flexible endoscopes without a working channel between UV-C light disinfection versus standard endoscope Washer Disinfection: a randomized controlled trial.

Background: To prevent cross-contamination between patients, adequate reprocessing is necessary when using flexible endoscopes (FEs) without a working channel. The current reprocessing process using an Endoscope Washer Disinfector (EWD) is time-consuming. Ultraviolet light group C (UV-C) exposition is an alternative and fast disinfection method and has previously been shown to adequately reduce Colony Forming Units (CFUs) on FEs without a working channel.

Heterodimer Formation of the Homodimeric ABC Transporter OpuA.

Many proteins have a multimeric structure and are composed of two or more identical subunits. While this can be advantageous for the host organism, it can be a challenge when targeting specific residues in biochemical analyses. In vitro splitting and re-dimerization to circumvent this problem is a tedious process that requires stable proteins.

In silico method for selecting residue pairs for single-molecule microscopy and spectroscopy.

Obtaining (dynamic) structure related information on proteins is key for understanding their function. Methods as single-molecule Förster Resonance Energy Transfer (smFRET) and Electron Paramagnetic Resonance (EPR) that measure distances between labeled residues to obtain dynamic information rely on selection of suitable residue pairs for chemical modification. Selection of pairs of amino acids, that show sufficient distance changes upon activity of the protein, can be a tedious process.

Gating by ionic strength and safety check by cyclic-di-AMP in the ABC transporter OpuA.

(Micro)organisms are exposed to fluctuating environmental conditions, and adaptation to stress is essential for survival. Increased osmolality (hypertonicity) causes outflow of water and loss of turgor and is dangerous if the cell is not capable of rapidly restoring its volume. The osmoregulatory adenosine triphosphate-binding cassette transporter OpuA restores the cell volume by accumulating large amounts of compatible solute.

Membrane Lipid Requirements of the Lysine Transporter Lyp1 from Saccharomyces cerevisiae.

Membrane lipids act as solvents and functional cofactors for integral membrane proteins. The yeast plasma membrane is unusual in that it may have a high lipid order, which coincides with low passive permeability for small molecules and a slow lateral diffusion of proteins. Yet, membrane proteins whose functions require altered conformation must have flexibility within membranes.

Periprotein lipidomes of provide a flexible environment for conformational changes of membrane proteins.

Yeast tolerates a low pH and high solvent concentrations. The permeability of the plasma membrane (PM) for small molecules is low and lateral diffusion of proteins is slow. These findings suggest a high degree of lipid order, which raises the question of how membrane proteins function in such an environment.

A synthetic metabolic network for physicochemical homeostasis.

One of the grand challenges in chemistry is the construction of functional out-of-equilibrium networks, which are typical of living cells. Building such a system from molecular components requires control over the formation and degradation of the interacting chemicals and homeostasis of the internal physical-chemical conditions. The provision and consumption of ATP lies at the heart of this challenge.

Cell Fuelling and Metabolic Energy Conservation in Synthetic Cells.

We are aiming for a blue print for synthesizing (moderately complex) subcellular systems from molecular components and ultimately for constructing life. However, without comprehensive instructions and design principles, we rely on simple reaction routes to operate the essential functions of life. The first forms of synthetic life will not make every building block for polymers de novo according to complex pathways, rather they will be fed with amino acids, fatty acids and nucleotides.

High-Throughput Simulations Reveal Membrane-Mediated Effects of Alcohols on MscL Gating.

The mechanosensitive channels of large conductance (MscL) are bacterial membrane proteins that serve as last resort emergency release valves in case of severe osmotic downshock. Sensing bilayer tension, MscL channels are sensitive to changes in the bilayer environment and are, therefore, an ideal test case for exploring membrane protein coupling. Here, we use high-throughput coarse-grained molecular dynamics simulations to characterize MscL gating kinetics in different bilayer environments under the influence of alcohols.