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Folding and association of β-galactosidase


Nichtl, Alfons ; Buchner, Johannes ; Jaenicke, Rainer ; Rudolph, Rainer ; Scheibel, Thomas:
Folding and association of β-galactosidase.
In: Journal of Molecular Biology. Bd. 282 (Oktober 1998) Heft 5 . - S. 1083-1091.
ISSN 0022-2836
DOI: https://doi.org/10.1006/jmbi.1998.2075


β-d-Galactosidase from Escherichia coli is one of the largest tetrameric enzymes known at present. Although its physiological importance, the regulation of its synthesis, its enzymatic properties and its structure are well established, little is known about the stability and the folding pathway of this enzyme. Here we show that the overall folding mechanism of chemically denatured β-galactosidase consists of three stages: (i) formation of elements of secondary structure; (ii) collapse to subdomains and structured monomers; (iii) association to the native quaternary structure via dimeric intermediates. The first rate-limiting step is the association of structured monomers to form dimers in a bi-molecular reaction, with a rate constant of 4.3×103 M−1 s−1at 20°C. The second rate-limiting uni-molecular folding step leads to dimers which are competent for further association, with a rate constant of 0.5×10−3 s−1at 20°C. Tetramers form from these dimers in a fast reaction. By determining a similar mechanism for α-complementation of β-galactosidase fragments it could be confirmed that β-galactosidase follows a consecutive bi-uni-molecular mechanism of folding and association.

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Publikationsform: Artikel in einer Zeitschrift
Begutachteter Beitrag: Ja
Keywords: α-complementation; protein stability; chaperones
Institutionen der Universität: Fakultäten
Fakultäten > Fakultät für Ingenieurwissenschaften
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien
Fakultäten > Fakultät für Ingenieurwissenschaften > Lehrstuhl Biomaterialien > Lehrstuhl Biomaterialien - Univ.-Prof. Dr. Thomas Scheibel
Profilfelder > Advanced Fields > Neue Materialien
Profilfelder > Advanced Fields > Molekulare Biowissenschaften
Profilfelder > Advanced Fields > Polymer- und Kolloidforschung
Profilfelder > Emerging Fields > Lebensmittel- und Gesundheitswissenschaften
Profilfelder > Advanced Fields
Profilfelder > Emerging Fields
Titel an der UBT entstanden: Nein
Themengebiete aus DDC: 600 Technik, Medizin, angewandte Wissenschaften
600 Technik, Medizin, angewandte Wissenschaften > 620 Ingenieurwissenschaften
Eingestellt am: 01 Okt 2015 12:45
Letzte Änderung: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/20055