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Join us as PhD in Applied Life Sciences student Karen Mendivil speaks about: Decoding Intrinsically Disordered Protein – Glycosaminoglycans Interactions and their Relevance in Health and Disease
Intrinsically disordered proteins (IDPs) and intrinsically disordered regions (IDPRs) are present in many proteomes and are involved in various cellular processes. The structural plasticity of IDPs/IDPRs provides functional diversity to proteins; hence this data set of proteins is involved in pathologies such as cancer, neurodegenerative disorders, viral infections, and others. It has been proposed that pathological changes of IDPs/IDPRs are triggered by structural rearrangements of post-translational modifications (PTMs) and their transient interaction with other molecular partners. On the other hand, glycosaminoglycans (GAGs) are components of the extracellular matrix, and they interact with several proteins at the cell surface and in the extracellular matrix. In this context, GAGs have been found to bind to a variety of proteins with diverse functions and play a crucial role in cell signaling process. Previously, the relationship between the affinity of GAGs-protein interactions and the amount of intrinsic disorder in GAGs binding proteins has been investigated; however, the specific pattern of binding of glycosaminoglycans in families of conserved families of IDPRs is not well understood yet. This seminar aims to present and discuss experimental and computational approaches that allow the study of GAGs-IDPRs interactions and physicochemical parameters that drive these interactions.