2-Methyltetrahydrofuran and cyclopentylmethylether: two green solvents for efficient purification of membrane proteins like FhuA.

β-Barrel shaped membrane proteins are attractive hosts for hybrid catalysts in which reactions are controlled through space. Production and extraction of β-barrel shaped membrane proteins in gram scale is challenging due to their hydrophobicity. Solvent mixtures such as chloroform/methanol (CM) are widely used for membrane protein extraction but toxicity and mutagenicity were reported in several cases.

A hybrid ring-opening metathesis polymerization catalyst based on an engineered variant of the β-barrel protein FhuA.

A β-barrel protein hybrid catalyst was prepared by covalently anchoring a Grubbs-Hoveyda type olefin metathesis catalyst at a single accessible cysteine amino acid in the barrel interior of a variant of β-barrel transmembrane protein ferric hydroxamate uptake protein component A (FhuA). Activity of this hybrid catalyst type was demonstrated by ring-opening metathesis polymerization of a 7-oxanorbornene derivative in aqueous solution.

First insights on organic cosolvent effects on FhuA wildtype and FhuA Δ1-159.

Circular dichroism (CD) and deconvolution were used to study the structural integrity of a "plugged" and an "open" FhuA transmembrane channel protein in the presence of varied concentrations of tetrahydrofuran (THF), ethanol (EtOH) and chloroform/methanol (C/M). FhuA is an Escherichia coli outer membrane protein (78.9 kDa) consisting of 22 β-sheets and an internal globular cork domain which acts as an iron transporter.

Interspecific resource competition-combined effects of radiation and nutrient limitation on two diazotrophic filamentous cyanobacteria.

The cyanobacterial blooms in the Baltic Sea are dominated by diazotrophic cyanobacteria, the potentially toxic species Aphanizomenon sp. and the toxic species Nodularia spumigena. The seasonal succession with peaks of Aphanizomenon sp.