Autor:	Stephan N. Witt, Sergey V. Slepenkov
Rok vydání:	1999
Předmět:	Sociology and Political Science biology Chemistry Clinical Biochemistry Kinetics Peptide binding Biochemistry Fluorescence Clinical Psychology Tryptophan fluorescence Chaperone (protein) biology.protein Chaperone activity Law Spectroscopy Social Sciences (miscellaneous)
Zdroj:	Journal of Fluorescence. 9:281-293
ISSN:	1053-0509
DOI:	10.1023/a:1020531923349
Popis:	This article reviews the recent progress in unraveling the kinetic mechanism of the 70-kDa molecular chaperones by the use of fluorescence spectroscopic methods. Dissecting the kinetics of the individual steps in the 70-kDa chaperone reaction cycle in vitro—ATP binding, peptide binding, interdomain coupling, and chaperone-catalyzed ATP hydrolysis—provides a foundation which can be used to develop a clear understanding of the molecular basis for chaperone activity in vivo.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::f4f7f903ec46dbfa87c0171848b63835 https://doi.org/10.1023/a:1020531923349 Zobrazit plný text záznamu Full text from SpringerLink