Structure and hydride transfer mechanism of a moderate thermophilic dihydrofolate reductase from Bacillus stearothermophilus and comparison to its mesophilic and hyperthermophilic homologues.

Dihydrofolate reductase (DHFR) from a moderate thermophilic organism, Bacillus stearothermophilus, has been cloned and expressed. Physical characterization of the protein (BsDHFR) indicates that it is a monomeric protein with a molecular mass of 18,694.6 Da (0.

A Synthetic Pore-Mediated Transmembrane Transport of Glutamic Acid.

Transported to the other side: Cyclic D,L-α-peptides self-assemble in lipid bilayers into transmembrane ion channels that may allow efficient transport of glutamic acid. The molecular transport is size/shape selective, as evidenced by the high transport rates observed with cyclodecapeptide-based transmembrane pores but not with the smaller cyclooctapeptide analogue.