[Study of the conformation of neurospecific cardioactive glycoproteins by optical spectroscopy]

Using selective fluorescence quenching and circular dichroism techniques, the conformation of protein carriers of earlier detected cardiotropic hypothalamic neurohormones was investigated. The experimental results point to essential differences in the structural organization of the above compounds that were designated according to the type of their binding to corresponding hormones as BNH, BNC and BNS. For instance, the circular dichroism spectrum of BNS is typical of proteins that are characterized by a high content of non-ordered structures, a low content of beta-structures and an almost complete absence of alpha-helices. BNC and BNH with nearly the same content of alpha-helical structures are distinguished by the number of "non-ordered glomes" which are more abundant in BNC. These results are in good agreement with the fluorescence quenching data.