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  • Residue interaction networks

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    Proteins, as large macromolecules, exhibit intricate three-dimensional structures and dynamic motions that enable them to perform various cellular functions. These functions rely on non-covalent interactions, which contribute to the stability of folded structures, facilitate interactions with other molecules, and play vital roles in molecular communication, such as allosterism and signaling processes, often mediated by transient…

  • Protein aggregation

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    The formation of amyloid aggregates upon protein misfolding is related to several devastating degenerative diseases. We developed PASTA to predict the propensities of protein sequences to aggregate into amyloids. These propensities represent the presence of aggregation hot spots stabilizing pathological interactions, the establishing of cross-amyloid interactions between co-aggregating proteins and the stability of the amyloid…