Biomedical subjects

N Tuparev

Publications and source records attributed to N Tuparev.

3 recordsLinked to original sources

PubMed2003

Irreversible temperature-induced changes in purple membranes studied by electrooptics.

The thermal stability of purple membranes is studied by electric light scattering. Information on the polarization mechanisms is obtained. Incomplete recovery of the initial electric state (i.e., of permanent dipole moment, p( perpendicular), and electric polarizability, gamma(fast, ||)) after the membranes are heated at temperatures above 60 degrees C is revealed. Additional slow polarizability components, gamma(slow, perpendicular) and gamma(slow, ||), relaxing at different characteristic frequencies than the fast longitudinal polarizability gamma(fast, ||) appear in the temperature range where the order-disorder transition takes place. The slow polarizability gamma(slow, perpendicular) is probably connected with counterion displacement in the electrical double layer perpendicular to the disk plane. The results are important for understanding the polarization mechanisms and the origin of slow orienting moments.

Electrochemistry↗

PubMed2001

Buffer-induced changes of purple membrane surface electric properties: an electro-optical study.

Buffer-induced alteration of the purple membrane electric dipole moments and electrokinetic charge was studied by electric light scattering and microelectrophoresis. The permanent dipole moment and electrophoretic mobility of purple membranes change in opposite direction in presence of 'P'- and 'N'-type buffer molecules, shown to produce 'positive' and 'negative' additional components to the bR light-induced charge displacement current. It is concluded that the two types buffer molecules distribute differently on the membrane surfaces, depending on their protonation state, as a result of different interaction with the membrane cytoplasmic and extracellular surfaces.

Journal Article↗

PubMedDate not supplied

Bacteriorhodopsin thermal stability: influence of bound cations and lipids on the intrinsic protein fluorescence.

Temperature-induced changes in protein intrinsic fluorescence of native, delipidated and deionized purple membranes are investigated. It is found that the removal of cations most strongly affects the protein and its thermal stability. The denaturation of dei-BR completes at 70 degrees C, while delipidated and native BR still maintain their native structure at this temperature. Both the quantum yield and the fluorescence maximum suggest correlation between the Trp-retinal coupling and protein structural stability. The low red shift of the fluorescence maximum caused by increasing of temperature indicates limited unfolding of bacteriorhodopsin upon denaturation.

Bacteriorhodopsins↗