"Компьютерные решения Siemens для научных исследований"
Л.В. Клюев, О.В. Михеев
Catalyst Silicon Solutions
"Перенос электрона на большое расстояние в белках"
В.Д.Лахно
Институт математических проблем биологии РАН
В докладе обсуждается проблема электронного переноса в химических и биологических системах. Дается обзор современного состояния теоретических и экспериментальных исследований по переносу электрона в белках. Сформулирована новая концепция переноса электрона через протяженные электронные состояния коллективного типа. Показано, что перенос электрона через коллективные электронные возбуждения является альтернативным суперобмену через химические связи для внутрибелкового электронного транспорта и доминирующим в реакциях самообмена белков. Полученные результаты удовлетворительно согласуются с экспериментальными данными по реакциям самообмена между глобулярными белками.
"Синтез и исследование меченых 3H аминокислот , пептидов и белков с использованием твердофазных реакций"
Золотарев Ю.А.
Институт молекулярной генетики РАН.
"Latent Periodicity Of Protein And DNA Sequences."
Eugene V. Korotkov
Centre of Bioengineering Russian Academy of Sciences
The mathematical method for the search of a latent periodicity in protein and DNA sequences has been developed. Latent periodicity is periodicity when the gomology between periods is very low or absent. It is difficult to find the latent periodicity by all early developed mathematical methods. More than 10% proteins from SWISS-PROT data bank has regions with latent periodicity. As example the latent periodicity was revealed in the next proteins: lipoamide dehydrogenase of Azotobacter vinelandii from DLDH_AZ VI clone, Glutamine-dependent asparagine synthetase from ASN1_YEAST clone, Endochitinase 2 of CHI2_COCIM clone, Citron protein from CTRO-MOUSE clone. These protein sequences have latent periodicity equal to 19, 6, 11, and 7 amino acids, correspondingly. The possible significance of protein sequence latent periodicity is discussed.
"Hydration and equilibrium dynamics of proteins at normal and high pressure"
Dr. D. Kharakoz
Institute of Protein Research
"Molecular dynamics of proteins and electron-conformational interactions"
Dr. Konstantin V. Shaitan
Moscow State University,
Biological Department
The fundamental physical principles of the dynamical behavior of biomacromolecules is discussed. The Mossbauer spectroscopy data, electron transfer and the data on ligand diffusion in proteins were among the starting points of this report. The concept based on topological structure peculiarities of potential energy level hypersurfaces of limited diffusion on conformational substates for internal protein dynamics is reinstalled. Molecular dynamics of the serious of modified dipeptides are investigated. The methods of dihedral angles dynamical correlation functions and free energ y maps calculation are introduced. These correlation functions and free energy maps can characterize the dynamical properties of peptides in details. The dynamical symmetry in the serious of biological important aminoacids is developed. The dynamical properties of biological important aminoacid residues and defective ones are compared. Atomic charges variations during conformational fluctuations in aminoacids residues are investigated. The general concept of electron-conformational interactions and protein functioning are discussed.
"Intermediate states of protein molecules and their biological role"
Dr. Valentina E. Bychkova
Institute of Protein Research,
Russian Academy of Sciences
"Folding rate and folding nucleus in protein structure"
Dr. Alexey V. Finkelstein
Institute of Protein Research,
Russian Academy of Sciences
We show that a nucleation and growth pathway having a low transition sta te free energy leads to the most stable fold of a protein chain. The transition state free energy on these pathways depends mostly on the surface effects and hence is proportional to N^2/3 rather to N, the number of chain residues. As a result, the most stable fold can be normally achieved within ~exp(N^2/3) ns (rather than in ~10^N, according to the famous paradoxical Levinthal's estimate), which means that the most stable structure of a chain of N~100 residues can be normally achieved within seconds (rather than in 10^80 years according to Levinthal). Fast folding takes place close to the point of an "all-or-none" transition from the disordered to the native state: here all the misfolded structures are unstable relatively to the starting disordered state and hence cannot "trap" the folding. The transition states for folding of different proteins are considered. The corresponding folding nuclei are found in the 3D protein folds using a dynamic programming like method. It is shown that the position of a nuclei in the 3D fold depends on the fold.s shape rather than on the detaile interaction energies. A comparison with the data of protein engineering experiments shows an accuracy of the theory. Implementation of these results to protein structure prediction is discussed.
"Diversity of compact denaturated states in proteins"
Dr. Vladimir N. Uversky
Institute of Protein Research,
Russian Academy of Sciences
"Molecular modeling of membrane-bound domains in proteins"
Dr. Roman G. Efremov
M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic
Chemistry,
Russian Academy of Sciences