Search for dissertations about: "Daniel Otzen"
Showing result 1 - 5 of 6 swedish dissertations containing the words Daniel Otzen.
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1. Protein Misfolding in Human Diseases
Abstract : There are several diseases well known that are due to aberrant protein folding. These types of diseases can be divided into three main categories:Loss-of-function diseasesGain-of-toxic-function diseasesInfectious misfolding diseases Most loss-of-function diseases are caused by aberrant folding of important proteins. READ MORE
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2. The Folding Energy Landscape of MerP
Abstract : This thesis is based on studies, described in four papers, in which the folding energy landscape of MerP was investigated by various techniques. MerP is a water-soluble 72 amino acid protein with a secondary structure consisting of four anti-parallel β-strands and two α-helices on one side of the sheet in the order β1α1β2β3α2β4. READ MORE
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3. Molecular Mechanisms of Folding and Binding in PDZ Domains
Abstract : PDZ domains are one of the most abundant protein-protein interaction modules that mediate protein recognition by binding to short amino acid sequences in the cells. These globular protein domains usually consist of 80-100 amino acid residues that fold into six ß-strands and two a-helices. READ MORE
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4. Characterization and Engineering of Protein-Protein Interactions Involving PDZ Domains
Abstract : The work presented in this thesis has contributed with knowledge to several aspects of protein-protein interaction involving PDZ domains. A substantial amount of our proteome contains regions that are intrinsically disordered but fold upon ligand interaction. READ MORE
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5. Self-assembly of amyloid-β peptides in the presence of metal ions and interacting molecules – a detour of amyloid building blocks
Abstract : Misfolding of proteins into amyloid structures is implicated as a pathological feature in several neurodegenerative diseases and the molecular causes are still unclear. One typical characteristic of Alzheimer’s disease is self-assembly and accumulation of soluble amyloid-β (Aβ) peptides into insoluble fibrils and plaques. READ MORE