The three dimensional structure of a pheromone binding protein from Bombyx mori complexed with its substrate was determined recently [Sandler et al., Chem. Biol. 7, 143-151 (2000)]. The structure suggested that a loop formed by amino acid residues 60-69 could serve as a flexible lid into the pheromone binding pocket. To examine the above hypothesis, a molecular dynamics simulation was performed for a substrate free form of the protein starting from the crystal structure. In the simulation loop 60-69 took a conformation different from that in the substrate bound form. Also, the loop was the most flexible region of the protein. Thus, the simulation supports the hypothesis that the loop is a flexible lid.

N-Substituted-1,3,5-trimethylcyclohexane-3,5-imido-1-carboxylic acids efficiently transported CaII and MgII from alkaline earth metal ion mixtures against their concentration gradient through a chloroform liquid membrane.

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