Sökning: "intrinsically disordered protein"
Visar resultat 1 - 5 av 48 avhandlingar innehållade orden intrinsically disordered protein.
1. Biophysical characterization of protein-protein interactions involving intrinsically disordered proteins
Sammanfattning : Intrinsically disordered proteins and regions (IDPs/Rs) are proteins that do not form stable and well-defined structures in their free states but rather occupy an ensemble of conformations that change over time while still staying functional. They are prevalent in the eukaryotic proteome and are involved in various vital processes in the cell where they often interact with their binding partners through coupled binding and folding reactions. LÄS MER
2. Evolution of Interactions Involving Intrinsically Disordered Proteins
Sammanfattning : This thesis describes the evolution of intrinsically disordered proteins and their interaction partners. The work presented is a combination of phylogenetic analysis, ancestral reconstruction and biophysical characterization in order to examine the evolutionary trajectory of protein-protein interactions involving disorder. LÄS MER
3. Evolution and Binding Mechanisms of Intrinsically Disordered Proteins
Sammanfattning : Intrinsically disordered proteins (IDPs) make up a considerable fraction of the proteome in eukaryotic organisms. These proteins often act as hubs in interaction networks, harbouring multiple interaction with other proteins, and thus evolution has to walk a tightrope to accommodate new interactions while maintaining the previously established interactions. LÄS MER
4. Exploring small heat shock protein chaperones by crosslinking mass spectrometry
Sammanfattning : Together with other molecular chaperones, small heat shock proteins are key components of the protein quality control system, which is comprised of several hundred proteins and acts to maintain proteome homeostasis in the cell. Small heat shock proteins bind unfolding proteins at an early stage, to prevent these from further unfolding and aggregating. LÄS MER
5. From protein sequence to structural instability and disease
Sammanfattning : A great challenge in bioinformatics is to accurately predict protein structure and function from its amino acid sequence, including annotation of protein domains, identification of protein disordered regions and detecting protein stability changes resulting from amino acid mutations. The combination of bioinformatics, genomics and proteomics becomes essential for the investigation of biological, cellular and molecular aspects of disease, and therefore can greatly contribute to the understanding of protein structures and facilitating drug discovery. LÄS MER
