Positive cooperativity in the functioning of molecular chaperone GroEL

Autor:	E S, Bochkareva, N M, Lissin, G C, Flynn, J E, Rothman, A S, Girshovich
Rok vydání:	1992
Předmět:	Adenosine Triphosphate Bacterial Proteins Adenine Nucleotides Protein Conformation Hydrolysis Chaperonin 10 Escherichia coli Chaperonin 60 Ligands Heat-Shock Proteins Thiosulfate Sulfurtransferase
Zdroj:	The Journal of biological chemistry. 267(10)
ISSN:	0021-9258
Popis:	In the presence of its partner, GroES, the tetradecameric molecular chaperone GroEL binds 14 ATP molecules, half of which are hydrolyzed in a cooperative manner. Moreover GroEL can bind, with a positive cooperativity, more than two molecules of nonfolded protein rhodanese. The role of the cooperative mechanism in the functioning of GroEL is discussed.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::b1f2f5823cd56ac22b70e1255faf6e17 https://pubmed.ncbi.nlm.nih.gov/1348056 Zobrazit plný text záznamu