Solution x-ray-scattering study on the chaperonin groel from escherichia-coli

Autor:	Kaoru Ichimura, Shigeru Matsuzaki, Teikichi Ikura, Yoshihiko Igarashi, Hiroshi Kihara, Kazumoto Kimura, Kunihiro Kuwajima
Rok vydání:	1995
Předmět:	Protein Conformation Scattering Chemistry X-Rays Organic Chemistry Biophysics X-ray Chaperonin 60 Radius medicine.disease_cause Biochemistry GroEL Chaperonin Solutions Crystallography Models Chemical Escherichia coli medicine Radius of gyration Scattering Radiation Molecule
Zdroj:	Biophysical Chemistry. 53:259-266
ISSN:	0301-4622
DOI:	10.1016/0301-4622(94)00107-u
Popis:	The molecular architecture of native GroEL has been studied by solution X-ray scattering. The radius of gyration for the native molecule was estimated to be 66.0 A in 50 mM Tris-HCl, 100 mM KCl at pH 7.5 and 25°C. The maximum dimension was estimated to be 170 A, based on the pair distance distribution function. A cylindrical structure or two heptameric rings was found to be the best for native GroEL among structures examined by using a multi-sphere model analysis in which the radius of constituent sphere was 6 A. The results of the model analysis show that the radius of GroEL is 68.0 A and the height is 150.7 A. Unexpectedly, the central penetrating hole through GroEL was not confirmed in the best-fit structure.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e469b7ce8bcc4d4280c4bce079b13c19 https://doi.org/10.1016/0301-4622(94)00107-u Zobrazit plný text záznamu Full Text from ScienceDirect