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Conservation of the folding mechanism between a thermostable (βα)8-barrel enzyme, its evolutionary relatives, and ancestral precursors generated by protein design

Carstensen, Linn (2012) Conservation of the folding mechanism between a thermostable (βα)8-barrel enzyme, its evolutionary relatives, and ancestral precursors generated by protein design. PhD, Universität Regensburg.

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Date of publication of this fulltext: 05 Nov 2012 07:25

Abstract (English)

The (βα)8-barrel is amongst the most ancient, frequent and versatile enzyme folds. Sequence and structure comparisons suggest that modern (βα)8-barrels have divergently evolved from a common ancestor, which raises the question whether they share the same folding mechanism. Here, this problem was appraoched by using the thermostable cyclase subunit HisF of imidazole glycerol phosphate (ImGP) ...

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Translation of the abstract (German)

Das (βα)8-barrel gehört zu den ursprünglichsten, vielseitigsten und häufigsten Faltungstypen bekannter Proteine. Sequenz- und Strukturvergleiche legen nahe, dass (βα)8-barrel Enzyme das Produkt einer divergenten Evolution ausgehend von einem gemeinsamen Vorläufer sind. Daraus ergibt sich die Frage, ob alle Vertreter einen gemeinsamen Faltungsmechanismus aufweisen. Die thermostabile ...

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Item type:Thesis of the University of Regensburg (PhD)
Date:5 November 2012
Referee:Prof. Dr. Reinhard Sterner
Date of exam:15 October 2012
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Classification:
NotationType
BiowissenschaftenUNSPECIFIED
Keywords:protein folding, design and evolution, kinetic stabilization, thermostability, Proteinfaltung, Proteindesign, Proteinevolution, Thermostabilität, kinetische Stabilität
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:26555
Owner only: item control page

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