vavilovВавиловский журнал генетики и селекцииVavilov Journal of Genetics and Breeding2500-3259Institute of Cytology and Genetics of Siberian Branch of the RASvavilov-74Research ArticleСтатьиArticlesКОМПЬЮТЕРНЫЕ МЕТОДЫ ИССЛЕДОВАНИЯ ТЕРМОСТАБИЛЬНОСТИ БЕЛКОВ И ИХ ПРИМЕНЕНИЕ В БИОЛОГИИTHEORETICAL METHODS FOR INVESTIGATING PROTEIN THERMOSTABILITY AND THEIR APPLICATIONS IN BIOLOGYАлемасовН. А.AlemasovN. A.alemasov@bionet.nsc.ruФоминЭ. С.FominE. S.alemasov@bionet.nsc.ruФедеральное государственное бюджетное научное учреждение «Федеральный исследовательский центр Институт цитологии и генетики Сибирского отделения Российской академии наук», Новосибирск, РоссияРоссияInstitute of Cytology and Genetics SB RAS, Novosibirsk, RussiaRussian Federation201215122014164/1774783Copyright © Алемасов Н.А., Фомин Э.С., 20142014Алемасов Н.А., Фомин Э.С.Alemasov N.A., Fomin E.S.This work is licensed under a Creative Commons Attribution 4.0 License.https://vavilov.elpub.ru/jour/article/view/74

Проведена классификация существующих теоретических подходов к исследованию термостабильности белков. Методы компьютерного моделирования динамики белков позволяют наиболее полно оценить микро- и макропараметры исследуемых молекул, но без уточнений (например, в части учета распределения заряда) они ограничены в точности получаемых результатов. Перспективными ввиду низкой требовательности к вычислительным ресурсам являются также методы выделения жестких фрагментов белков. Они позволяют напрямую определить изменения в гибкости структуры при совершении аминокислотных замен. Но их недостатком является сложность оценки влияния окружающего растворителя и его термодинамических параметров.

Classification of existent theoretical approaches for investigating protein thermal stability is performed. Computer simulations allow to fully estimate micro- and macro properties of the molecules. But those approaches are limited in accuracy and therefore require certain improvements e.g. making them to allow for molecular charge distribution. Also promising methods are those dealing with rigid regions of proteins. They do not require a huge amount of computations and allow to directly determine changes in molecular structure flexibility caused by mutated amino acid residues. But using the only structure it is impossible to explicitly estimate an effect of solvent and its thermodynamical properties.

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The authors declare that there are no conflicts of interest present.