Identifying Metal Binding Sites in Proteins Using Homologous Structures, the MADE Approach.

In order to identify the locations of metal ions in the binding sites of proteins, we have developed a method named the MADE (MAcromolecular DEnsity and Structure Analysis) approach. The MADE approach represents an evolution of our previous toolset, the ProBiS HO (MD) methodology, for the identification of conserved water molecules. Our method uses experimental structures of proteins homologous to a query, which are subsequently superimposed upon it.

Tetrahedrality, hydrogen bonding and the density anomaly of the central force water model. A Monte Carlo study.

Monte Carlo computer simulations in the canonical and grand canonical statistical ensemble were used to explore the properties of the central force (CF1) water model. The intramolecular structure of the HO molecule is well reproduced by the model. Emphasis was made on hydrogen bonding, and on the tehrahedral, , and translational, , order parameters.

Determination of traces of indium, manganese, arsenic and antimony in zinc by neutron-activation analysis.

Destructive activation determination of the trace elements indium, manganese, arsenic and antimony in different samples of pure zinc metal by solvent extraction techniques is described. Determination of indium and manganese is based on the quantitative co-precipitation of both elements with lanthanum hydroxide, followed by their extraction with sodium diethyldithiocarbamate in the presence of potassium cyanide and their subsequent separation by selective stripping. The quantitative determination of arsenic and antimony is based on the extraction of their iodides from sulphuric acid solution with toluene.

Trace element concentrations in higher fungi.

The concentrations of ten trace elements, As. Br, Cd, Cu, Hg I, Mn, Se, Zn and V, have been determined in up to 27 species of higher fungi from several sites in Slovenia, Yugoslavia. Analyses were based on destructive neutron activation techniques.