Kalinovsky P. Influence of extremely low frequency magnetic fields on hydrophobical interactions in protein solutions

It was researched hydrophobically dependent changes of structure and functional features of proteins which are dissolved in water under the influence of extra weak extremely low frequency magnetic fields. It is shown that magnetic field changes the dynamics of optical characteristics of solutions of proteins of the various nature as well as its structure and functional abilities in conditions of destabilizing factors and at interaction with hydrophobic ligands. Influence of this fields results in mismatching of synchronized dynamics of optical density for the proteins which have such synchronized dynamic in native solutions. Influence of extremely low frequency magnetic fields on interactions of albumin and cytochrome c with chlorophorm resultes acceleration and increasing of binding this ligand with pro-tein macromolecules. At the same time, such influence makes the probabilities of different spectral forms of albumin in water solution equal. Influence of such field temporarily reduces enzymatic activity of cytochrome c. Influence of extra low frequency magnetic fields to the binding of dissolved albumin with retinolacetate is of nonlinear character and depends on start concentration of retinolacetate. Statisti-cally approved effects (such as intensification of binding process) has been regis-tered in cases with extremely low and high concentrations of retinolacetate. The influence of ELF MF on process of interaction of albumin with tamoxyphen, with the help of increasing total positive signal of a difference between fluorescence of system "albumin-tamoxyphen" and tamoxyphen water solution, is established. The model explaining on a qualitative level the ELF MF influence on interaction of albuminous molecules with not polar low-molecular ligands in water solutions is offered.