About biopolymers, biotechnologies and drug production
For medicines and biotechnologies
Nikolay Podorvanyuk, "Newspaper.Ru»
Many people know about the importance of proteins, fats and carbohydrates in the processes of vital activity. At the same time, the so—called heterocyclic compounds (heterocycles) play an equally important role for living organisms - organic compounds containing cycles, which include other elements along with carbon. Heterocycles play an important role in the chemistry of natural compounds and biochemistry, many of them (quinine, morphine, pyramidone) are medicinal substances.
In addition, being widely distributed in wildlife, heterocycles can be valuable dyes (indigo), perform the functions of structure-forming polymers (cellulose derivatives) or be used in the production of plastics and in the vulcanization of rubber.
An article published this week in the Proceedings of the National Academy of Science is devoted to the research of one of these heterocyclic compounds — imidazole, which is a side residue of the amino acid histidine in protein molecules.
Structure and molecule of imidazole (C 3 H 4 N 2)
One of the authors of the publication is Yuri Vorobyov, chief researcher at the Novosibirsk Institute of Chemical Biology and Fundamental Medicine SB RAS, who told the newspaper.Ru" more about the work.
– What is the practical result of this work?
– This is an understanding of the fundamental foundations of the functioning of biopolymers, which opens up the possibility of designing more effective enzymes for biotechnologies or influencing the enzyme with the help of small molecules, i.e. creating drugs.
– What is the essence of your work?
– The amino acid histidine has unique properties (its side group – imidazole – is able to accept a proton, becoming positively charged, or transfer a proton from one nitrogen atom Nδ to another atom Nε, remaining neutrally charged). The equilibrium and relative content of different forms of imidazole depend on the three-dimensional structure of the protein molecule, the concentration of protons in solution and the properties of the solvent itself (polarity, salt, temperature, etc.) The amino acid histidine (sometimes there may be several) is located in the active centers of most enzymes and proteins, which are proton pumps regulating the concentration of protons in a living cell, that is, the acidity of the medium.
Determining the relative content of different forms of imidazole is an unsolved problem, important for understanding the mechanism of functioning of enzymes, which, as mentioned above, is of great practical importance.
Our work suggests a method for calculating the most probable states of imidazole depending on the 3D structure of the protein molecule and environmental characteristics. The calculation is carried out by combining the calculation of the probability of protonation of imidazole and experimental information on chemical shifts of carbon atoms in the imidazole ring.
– What is your contribution to the work published in PNAS?
– My contribution is the development of a method and a computer program for calculating electrostatic effects in biopolymers, in particular, calculating the degree of ionization of protein molecule groups. These calculations were made by me and are one of the elements of work in PNAS.
– Tell us more about the international team of scientists who worked on the article. When did the collaboration start, what are the plans for future research?
– Professor Harold Sheraga is one of the first founders of research on the principles of the structure of the 3D structure of protein molecules based on physical interactions between the atoms of the protein molecule and the surrounding solution. For the past 50 years, he has been leading a group of theorists and experimentalists at Cornell University of the State of New York, Ithaca. I first came to him in 1990, worked in this laboratory for four years and then worked in another group for six years – at the University of North Carolina at Chapel Hill, actually continuing cooperation with Professor Sheraga.
In 2001, I returned to Novosibirsk and continue to cooperate with colleagues from Professor Sheraga's group.
The first author of the current work is Jorge Villa from Argentina, we have known him since 1991. Another co–author, Elena Arnautova, is a Russian, she graduated from Moscow State University, but could not gain a foothold in Russia, has been working in the USA for more than 10 years. Over the past 5 years, we have published several articles in this author's composition. Joint work will continue as we complement each other's capabilities.
– You have been working abroad for several years, and now you are working in Russia. Do you agree with the statement that difficult times have come in Russian science now? Or do you manage to do science normally in Russia, without thinking about working abroad?
– Difficult times, I think, are behind us, in the 1990s, when it was really impossible to work, there were no necessary computers, devices, reagents and a decent salary. Personally, I am more comfortable working in Russia now, as a Doctor of sciences and chief researcher.
Of course, there are many problems. The most important is the financing of graduate students' work and the possibility of their material support. Funding through grants is unstable and, to put it mildly, their distribution is not always fair, because the stage of reviewing and expert evaluation of grants is not transparent. There are laboratories where grants are all right. But in general, neither the Academy of Sciences nor the government adequately solves the problem of sustainable and continuous training of graduate students.
In the USA, a graduate student is able to live on a postgraduate scholarship. This is not possible in Russia. Therefore, many young people leave because they do not find reliable prospects in Russia.
Portal "Eternal youth" http://vechnayamolodost.ru25.03.2011