Physicochemical Characteristics of a Variant of Chaperon GroEL Apical Domain Designed to Enhance the Expression and Stability of Target Proteins

Abstract: This work describes the properties of a new protein, a modification of GroEL apical domain designed to be a leader in fusion systems. This polypeptide leader demonstrates a high level of expression in a bacterial system; it is soluble and retains its solubility during standard biochemical manipulations. The secondary structure of the protein and its thermostability, as well as the protein solubility, were studied in a wide temperature range. To simplify the subsequent purification of the target protein, the possibility of its chemical cleavage from the fused protein by methionine residues with cyanogen bromide is provided. © 2019, Pleiades Publishing, Inc.

Авторы
Kurov K.A.2 , Savvin O.I.2 , Yurkova M.S. 2, 1 , Zenin V.A. 2, 1 , Nagibina G.S.3 , Melnik B.S.3 , Fedorov A.N. 2, 1
Номер выпуска
8
Язык
Английский
Страницы
765-770
Статус
Опубликовано
Том
55
Год
2019
Организации
  • 1 People’s Friendship University of Russia, Moscow, 117198, Russian Federation
  • 2 Fundamentals of Biotechnology Federal Research Center, Russian Academy of Sciences, Moscow, 119071, Russian Federation
  • 3 Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast 142290, Russian Federation
Ключевые слова
bacterial expression; chaperon GroEL; fusion system; leader protein
Дата создания
24.12.2019
Дата изменения
24.12.2019
Постоянная ссылка
https://repository.rudn.ru/ru/records/article/record/54823/
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