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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 ...

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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
Status:Published
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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