Scientific journal
Scientific Review. Biological science
ISSN 2500-3399
ПИ №ФС77-57454

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STRUCTURAL AND FUNCTIONAL FEATURES OF CHAPERON GROEL

Grishkova M.V. 1
1 Shemyakin and Ovchinnikov Institute of Bioorganic Chemistry RAS
First chaperones and their functions in the process of folding have been studied on the example of protein Escherichia coli - GroEL and GroES. Over the past few years there were a lot of studies of the structural and functional features of the molecular chaperone GroEL. According to the latest data GroEL interacts with nonnative proteins, preventing their misfolding and aggregation. It is assumed that this process consists of three stages: first, GroEL captures polipeptid chain, then the links between GroES and ATP, then the protein is inside the chaperone and folding of the protein occurs. After hydrolysis of ATP, the solution is released polypeptide. This review summarizes information about the structure and functions of the molecular chaperone GroEL.