arXiv subjects
Publications and source records attributed to Yu. Nastishin.
We have presented computer simulations of conoscopic patterns occurring in optically uniaxial gyrotropic crystals in the vicinity of isotropic point for a number of sets of crystal parameters and orientations. The appearance of special directions characterized by equalization of linear and circular birefringences has been revealed.
We have performed for the first time micro-Raman studies of lysozyme crystals for the temperatures lower than the room one (in the range 282-300K). Anomalous temperature dependence of the positions of Raman scattering bands has been detected and discussed, which corresponds to the crystalline lysozyme structure in the vicinity of T=285K.
It has been shown that conformational modifications of Hb induced by ethanol consumption can be visualized in optical spectra studying oxygenation kinetics of hemoglobin or mixing hemoglobin with Cibacron blue dye. Better dye affinity of blood proteins extracted from alcoholised rats with respect to those from non-alcoholised ones confirms that ethanol and its metabolites induce structural pathologies in blood protein molecules. The detected changes for the case of the posterity of intoxicated animals may be explained as a post-translation modification, as well as a disturbance of the structure and function of tissue cellular gene mechanism for the blood creation. It is established that alcohol intake during first four months leads to the decrease of fractional weight of oxyhemoglobin and to the increase of methemoglobin amount in blood. Further alcohol consumption is accompanied by recovering of the normal level of hemoglobin derivatives in blood. Normalization of the fractional weight of hemoglobin derivatives in blood after durable (longer than 5-6 months) ethanol intoxication is most probably due to the activation of the enzyme (acetaldehyde dehydrogenase) system, lowering the level of acetaldehydes in blood.
We present experimental evidence of the fact that lysozyme crystals, which are grown from their mother solution and exist in it, dissolve on heating above T=307 K. We argue that the anomaly in the light scattering recently observed at the temperature T=307 K and identified in the reference [Svanidze A. V. et al. 2006. JETP Lett. 84: 551] as a structural crystalline phase transition in the single lysozyme crystals, in fact, corresponds to a temperature limit of the crystal existence.