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Molecular Interactions and Macromolecular Assemblies

Protein folding and assembly are processes governed by a large number of non-covalent protein-protein interactions as well as interactions between the proteins and their environment. Within this area of research we study the relative contribution of different types of non-covalent interactions to protein folding and oligomerisation. Furthermore, we study the functional consequences of protein-ligand interactions and the regulation of these interactions. An intriguing aspect of protein self-assembly is the formation of amyloid fibrils, underlying several human diseases. At the Department we study proteins from Alzheimer, Parkinson and Huntington’s diseases. By designing self-assembling polypeptides we test our knowledge of factors controlling protein folding and association.

Principal investigator's involved in these projects: Sara LinseCecilia Emanuelsson.