Sökning: "Daniel Otzen"

Visar resultat 1 - 5 av 6 avhandlingar innehållade orden Daniel Otzen.

  1. 1. Protein Misfolding in Human Diseases

    Författare :Karin Almstedt; Per Hammarström; Daniel Otzen; Linköpings universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Misfolding; carbonic anhydrase; prion protein; protein stability; Biochemistry; Biokemi;

    Sammanfattning : 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. LÄS MER

  3. 2. The Folding Energy Landscape of MerP

    Författare :Ann-Christin Brorsson; Bengt-Harald Jonsson; Daniel Otzen; Umeå universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; Biochemistry; protein folding and stability; hydrogen exchange; intermediate; partial unfolding; Biokemi; Biochemistry; Biokemi; Biochemistry; biokemi;

    Sammanfattning : 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. LÄS MER

  4. 3. Molecular Mechanisms of Folding and Binding in PDZ Domains

    Författare :Syed Raza ul Haq; per jemth; Daniel Otzen; Uppsala universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES;

    Sammanfattning : 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. LÄS MER

  5. 4. Characterization and Engineering of Protein-Protein Interactions Involving PDZ Domains

    Författare :Andreas Karlsson; Per Jemth; Daniel Otzen; Uppsala universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; NATURVETENSKAP; NATURAL SCIENCES; intrinsically disordered protein regions; PDZ domain; binding kinetics; protein engineering; interaction mechanism; specificity; PDZbody; Chemistry with specialization in Biophysics; Kemi med inriktning mot biofysik;

    Sammanfattning : 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. LÄS MER

  7. 5. Self-assembly of amyloid-β peptides in the presence of metal ions and interacting molecules – a detour of amyloid building blocks

    Författare :Cecilia Mörman; Astrid Gräslund; Daniel Otzen; Stockholms universitet; []
    Nyckelord :NATURVETENSKAP; NATURAL SCIENCES; biophysics; Alzheimer’s disease; protein aggregation; amyloid formation; amyloid-β peptide; aggregation kinetics; interactions; metal ions; designed peptide constructs; Tau protein; NMR; circular dichroism; fluorescence spectroscopy; Biophysics; biofysik;

    Sammanfattning : 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. LÄS MER