电邮这篇文章 Engineering recombinant proteins: from structure to function and biological activity
- 作者: Dolgikh D.A1,2
-
隶属关系:
- Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS
- Lomonosov Moscow State University
- 期: 编号 7 (2025)
- 页面: 55-60
- 栏目: Review
- URL: https://ogarev-online.ru/0869-5873/article/view/305218
- DOI: https://doi.org/10.31857/S0869587325070063
- EDN: https://elibrary.ru/fiirks
- ID: 305218
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详细
The article discusses the development of recombinant protein engineering, primarily artificial proteins or de novo proteins, from the creation of the first proteins with a given spatial structure and biological activity to modern work in this area, which widely uses machine learning and artificial intelligence methods. The use of these methods, in particular the Rozetta and AlphaFold computer platforms, has led to tremendous progress in this area, as evidenced by last year’s Nobel Prize in Chemistry. Currently, these methods should be recommended for use in any modern laboratory conducting work on the physical chemistry of proteins and protein engineering.
作者简介
D. Dolgikh
Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS; Lomonosov Moscow State University
Email: dolgikh@nmr.ru
Moscow, Russia; Moscow, Russia
参考
- Долгих Д.А., Федоров А.Н., Чемерис В.В. и др. Получение и исследование альбебетина, искусственного белка с заданной пространственной структурой // Доклады АН. 1991. Т. 320. С. 1266–1269. Dolgikh D.A., Fedorov A.N., Chemeris V.V. et al. Production and study of albebetin, an artificial protein with a given spatial structure // Reports of the Academy of Sciences. 1991, vol. 320, pp. 1266–1269.
- Bychkova V.E., Dolgikh D.A., Balobanov V.A. et al. The Molten Globule State of a Globular Protein in a Cell Is More or Less Frequent Case Rather than an Exception // Molecules. 2022, vol. 27, no. 4361.
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- Finkelstein A.V., Ivankov D.N. Protein 3D Structure Identification by AlphaFold: a Physics-Based Prediction or Recognition Using Huge Databases? // Journal of Molecular Biology, 2024, vol. 6, pp. 1–10.
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