[Possibilities of wavelet-syncronization method for estimation of the spatial distribution of components of auditory evoked potentials in healthy subjects].

Event-related potentials (ERP) are informative indicators of higher nervous activity of healthy people and patients in pathological states. Traditionally, methods of ERP processing include peak-time characteristics, topographical mapping and localization of equivalent dipole sources. At the same time, estimation of ERP synchronization is complicated by a short duration of the process. The wavelet analysis makes it possible to overcome the disadvantages of the traditional Furrier analysis and to calculate characteristics of ERP synchronization, in particular, phase synchronization. A new approach to estimation of the auditory ERP in healthy persons is proposed in the article. The method is based on the analysis of phase wavelet-synchronization of ERP individual components under conditions of differentiation of different degrees of attention concentration in healthy persons.

[Interaction of cardiotoxin A5 with a membrane: role of conformational heterogeneity and hydrophilic properties]. / Vzaimodeistvie kardiotoksina A4 s membranoi: rol' konformatsionnoi geterogennosti i gidrofobnykh svoistv.

The hypothesis that local conformational differences of snake venom cardiotoxins (cytotoxins, CTs) may play a significant role in their interaction with membrane was tested by molecular modeling of the behavior of the CT A5 from the venom of Naja atra in water and at the water-membrane interface. Two models of the CT A5 spatial structure are known: the first was obtained by X-ray analysis and the second, by NMR studies in solution. A molecular dynamics (MD) analysis demonstrated that loop II of the toxin has a fixed omega-like shape in water, which does not depend on its initial structure. Interaction of the experimentally derived (X-ray and NMR) conformations and MD-simulated conformations of CT A5 with the lipid bilayer was studied by the Monte Carlo method using the previously developed model of the implicit membrane. The following was found: (1) Unlike the previously studied CT2 from the venom of cobra Naja oxiana, CT A5 has only loops I and II bound to the membrane, with the involvement of a lesser number of hydrophobic residues. (2) A long hydrophobic area is formed on the surface of CT A5 due to the omega-like shape of loop II and the arrangement of loop I in proximity to loop II. This hydrophobic area favors the toxin embedding into the lipid bilayer. (3) The toxin retains its conformation upon interaction with the membrane. (4). The CT A5 molecule has close values of the potential energy in the membrane and in an aqueous environment, which suggests a dynamic character of the binding. The results of the molecular modeling indicate a definite configuration of loops I and II and, consequently, a specific character of distribution of polar and apolar properties on the toxin surface, which turns out to be the most energetically favorable. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2003, vol. 29, no. 6; see also http://www.maik.ru.

[Modeling of peptides and proteins in membrane environment. I. A solvation model mimicking a lipid bilayer]. / Modelirovanie peptidov i belkov v membrannom okruzhenii. I.Model' sol'vatatsii, imitiruiushchaia lipidny'i bisloi.

A theoretical solvation model of peptides and proteins that mimics the heterogeneous membrane-water system was proposed. Our approach is based on the combined use of atomic parameters of solvation for water and hydrocarbons, which approximates the hydrated polar groups and acyl chains of lipids, respectively. This model was tested in simulations of several peptides: a nonpolar 20-mer polyleucine, a hydrophobic peptide with terminal polar groups, and a strongly amphiphilic peptide. The conformational space of the peptides in the presence of the membrane was studied by the Monte Carlo method. Unlike a polar solvent and vacuum, the membrane-like environment was shown to stabilize the alpha-helical conformation: low-energy structures have a helicity index of 100% in all cases. At the same time, the energetically most favorable orientations of the peptides relative to the membrane depend on their hydrophobic properties: nonpolar polyleucine is entirely immersed in the bilayer and the hydrophobic peptide with polar groups at the termini adopts a transbilayer orientation, whereas the amphiphilic peptide lies at the interface parallel to the membrane plane. The results of the simulations agree well with the available experimental data for these systems. In the following communications of this series, we plan to describe applications of the solvation model to membrane-bound proteins and peptides with biologically important functional activities.

[Modeling of peptides and proteins in a membrane environment.II. Structural and energetic aspects of Glycophorin A in a lipid bilayer]. / Modelirovanie peptidov i belkov v membrannom okruzhenii. II.Struktur nye i énergeticheskie aspekty glikoforina A v bisloe.

The conformational space of a hydrophobic peptide fragment of glycophorin A in a lipid membrane was studied with the Monte Carlo method using the solvation model described in the first communication of this series. The simulation was performed for various starting orientations of the peptide relative to the membrane bilayer: outside, inside, partially immersed, and transbilayer. We showed that the membrane substantially stabilizes the alpha-helical conformation of the central hydrophobic part of the glycophorin A molecule, which for the most part is immersed in the apolar core of the bilayer. For various conformational states, energy values were calculated and the orientations of the peptide relative to the membrane were characterized. Depending on the thickness of the bilayer, either an entirely alpha-helical conformation in transbilayer orientation or a conformation with a kink in the central part of the helix with the N- and C-termini exposed on one side of the membrane corresponds to the minimal-energy structure. The transmembrane orientation of glycophorin A is energetically advantageous when the membrane thickness is close to the length of its hydrophobic helical portion, which is consistent with the effect of "hydrophobic match" observed experimentally. The prospects for further refinement of the model are discussed.