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Tryptophan synthase complexes: evolution, substrate specificity, and quaternary structure

Busch, Florian (2016) Tryptophan synthase complexes: evolution, substrate specificity, and quaternary structure. PhD, Universität Regensburg.

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Date of publication of this fulltext: 02 Aug 2016 05:07

Abstract (English)

The permanent tryptophan synthase complex (TS) serves as a model system for the investigation of sophisticated protein-protein interactions. The permanent TS consists of a dimer of β-subunits and two α-subunits, which are located at both sites of the dimer, resulting in a αββα arrangement. The α-subunit catalyzes the aldolytic cleavage of indole-3-glycerol-phosphate (IGP). ...


Translation of the abstract (German)

Der permanente Tryptophansynthase Komplex (TS) dient als Modellsystem zur Untersuchung von hochentwickelten, sich wechselseitig regulierenden Protein-Protein Interaktionen. Der permanente TS besteht aus einem Dimer von β-Untereinheiten und zwei an beiden Seiten des Dimers assoziierten α-Untereinheiten, welche eine αββα-Anordnung ergeben. Die α-Untereinheit katalysiert die aldolytische Spaltung ...


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Item type:Thesis of the University of Regensburg (PhD)
Date:2 August 2016
Referee:Prof. Dr. Reinhard Sterner
Date of exam:24 July 2015
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Keywords:tryptophan synthase complex, O-phospho-L-serine, chimera design
Dewey Decimal Classification:500 Science > 570 Life sciences
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:32337
Owner only: item control page


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