Engineering recombinant proteins: from structure to function and biological activity

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Abstract

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.

The article is based on the author’s report at a scientific session of the Division of Biological Sciences of the Russian Academy of Sciences on December 10, 2024.

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About the authors

D. A. Dolgikh

Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry RAS; Lomonosov Moscow State University

Author for correspondence.
Email: dolgikh@nmr.ru

доктор биологических наук, профессор, руководитель лаборатории инженерии белка ИБХ РАН, профессор кафедры биоинженерии биофака МГУ

Russian Federation, Moscow; Moscow

References

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2. Fig. 1. The given spatial structure of the artificial protein albebetin

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3. Fig. 2. Artificial proteins based on albebetin with specified biological activities: A – blast-transforming activity (albeferon), B – anticancer activity, C – insulin-like activity, G and D – antiviral activity

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4. Fig. 3. From the Nobel Committee's press release on awarding the 2024 Nobel Prize in Chemistry to David Baker. Below: the structure of the artificial protein Top7 (left) and albebetin (right)

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