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Structural investigations of the Id helix-loop-helix dimerization domain

Kiewitz, Sebastian Donatus (2007) Structural investigations of the Id helix-loop-helix dimerization domain. PhD, Universität Regensburg.

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Date of publication of this fulltext: 12 Dec 2007 12:01

Abstract (English)

The Id proteins take part in many fundamental physiological processes during development and tumor-related events. A characteristic of these rather small proteins (119 up to 161 amino acids long) is a highly conserved dimerization domain, the helix-loop-helix (HLH) motif, which allows them to homo- or heterodimerize and makes them a subfamily of the large HLH protein family. Their preferred ...


Translation of the abstract (German)

Die Id Proteine sind an wichtigen physiologischen Prozessen, sowohl der normalen Entwicklung als auch der Tumorentstehung und -ausbreitung beteiligt. Ein Merkmal dieser eher kleinen Proteine (119 bis 161 Aminosäuren lang) ist ihre hoch konservierte Dimerisierungsdomäne, das Helix-Loop-Helix (HLH) Motiv, welches die Id Proteine zu der Familie der HLH Proteine zählen lässt und es ihnen ermöglicht ...


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Item type:Thesis of the University of Regensburg (PhD)
Date:11 December 2007
Referee:Prof. Dr. Armin Buschauer and Dr. Chiara Cabrele
Date of exam:June 2007
Institutions:Chemistry and Pharmacy > Institut für Organische Chemie > Alumni or Retired Professors > Arbeitskreis Dr. Chiara Cabrele
Chemistry and Pharmacy > Institute of Pharmacy > Pharmaceutical/Medicinal Chemistry II (Prof. Buschauer)
Keywords:Zirkulardichroismus , Fluoreszenzspektroskopie , Peptidsynthese , Helix-loop-Helix , Magnetische Kernresonanz , NMR-Spektroskopie , Id Proteine , Festphasenpeptidsynthese , Peptidanaloga , circular dichroism , fluorescence spectroscopy , solid-phase peptide synthesis , Id proteins
Dewey Decimal Classification:500 Science > 540 Chemistry & allied sciences
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:10584
Owner only: item control page


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